diff --git a/content/2.defense-systems/abi2.md b/content/2.defense-systems/abi2.md
index d13072925777a978ff9f3549b9f34db0bac62bb6..ec738837ea1a832d1307a7d46131dc59aa7eb9c0 100644
--- a/content/2.defense-systems/abi2.md
+++ b/content/2.defense-systems/abi2.md
@@ -1,12 +1,13 @@
 ---
 title: Abi2
 tableColumns:
-    article: 
+    article:
       doi: 10.1016/j.mib.2005.06.006
       abstract: |
-        Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
 ---
 
+# Abi2
 The Abi2 system is composed of one protein: Abi_2.
 
 Here is an example found in the RefSeq database: 
diff --git a/content/2.defense-systems/abia.md b/content/2.defense-systems/abia.md
index 2f2028ca815d99478a714ccf9626b4c9a262a82f..bd839a4ecb4885539bd315e05c2ab0e11ab8d085 100644
--- a/content/2.defense-systems/abia.md
+++ b/content/2.defense-systems/abia.md
@@ -4,9 +4,13 @@ tableColumns:
     article:
       doi: 10.1016/j.mib.2005.06.006
       abstract: |
-        Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiA
 The AbiA system have been describe in a total of 2 subsystems.
 
 Here is some example found in the RefSeq database:
diff --git a/content/2.defense-systems/abib.md b/content/2.defense-systems/abib.md
index c3ad1f3eae3df1a6b6ddb395dc674e9ae47480f9..79a37269f9eba0060d484cc7bfe2d274ed136aca 100644
--- a/content/2.defense-systems/abib.md
+++ b/content/2.defense-systems/abib.md
@@ -4,9 +4,13 @@ tableColumns:
     article:
       doi: 10.1016/j.mib.2005.06.006
       abstract: |
-        Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiB
 The AbiB system is composed of one protein: AbiB.
 
 Here is an example found in the RefSeq database: 
diff --git a/content/2.defense-systems/abic.md b/content/2.defense-systems/abic.md
index 5ab8dd9b6d2d8d81327ed6fc940c142158a6af0a..3cb3e6adfe8e0663089892b0e6e206b1e0d8938e 100644
--- a/content/2.defense-systems/abic.md
+++ b/content/2.defense-systems/abic.md
@@ -1,7 +1,16 @@
 ---
 title: AbiC
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiC
 The AbiC system is composed of one protein: AbiC.
 
 Here is an example found in the RefSeq database: 
diff --git a/content/2.defense-systems/abid.md b/content/2.defense-systems/abid.md
index 083702dd0d108d74372dc1a452c63cd5409cde50..6c6e543c8ab4f9f0ec3654b919fec05f520a00bd 100644
--- a/content/2.defense-systems/abid.md
+++ b/content/2.defense-systems/abid.md
@@ -1,7 +1,16 @@
 ---
 title: AbiD
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiD
 The AbiD system is composed of one protein: AbiD.
 
 Here is an example found in the RefSeq database: 
diff --git a/content/2.defense-systems/abie.md b/content/2.defense-systems/abie.md
index a3fac99810059ac5968574dda14f3da6b2bc7cf9..b47dbfdfa3cf2dd529e62358c3aa4dbab7c913fe 100644
--- a/content/2.defense-systems/abie.md
+++ b/content/2.defense-systems/abie.md
@@ -1,7 +1,16 @@
 ---
 title: AbiE
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiE
 AbiE is a family of an anti-phage defense systems. They act through a Toxin-Antitoxin mechanism, and are comprised of a pair of genes, with one gene being toxic while the other confers immunity to this toxicity. 
 
 It is classified as an Abortive infection system.
diff --git a/content/2.defense-systems/abig.md b/content/2.defense-systems/abig.md
index 3597e9b29588556721a933be24db9a02d2da0bd2..b4d91e2ebfe514629e15c23b3883ff525a3e1d63 100644
--- a/content/2.defense-systems/abig.md
+++ b/content/2.defense-systems/abig.md
@@ -1,7 +1,16 @@
 ---
 title: AbiG
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiG
 The AbiG system is composed of 2 proteins: AbiGi and, AbiGii.
 
 Here is an example found in the RefSeq database: 
diff --git a/content/2.defense-systems/abih.md b/content/2.defense-systems/abih.md
index 7560ae6e4c0461c5b9b492008255ce7d73b0d1be..2e67e94cd8641b15cf85ed6ed2054e739dc8a544 100644
--- a/content/2.defense-systems/abih.md
+++ b/content/2.defense-systems/abih.md
@@ -1,12 +1,16 @@
 ---
 title: AbiH
 tableColumns:
-    article: 
+    article:
       doi: 10.1111/j.1574-6968.1996.tb08446.x
       abstract: |
-        A gene which encodes resistance by abortive infection (Abi+) to bacteriophage was cloned from Lactococcus lactis ssp. lactis biovar. diacetylactis S94. This gene was found to confer a reduction in efficiency of plating and plaque size for prolate-headed bacteriophage φ53 (group I of homology) and total resistance to the small isometric-headed bacteriophage φ59 (group III of homology). The cloned gene is predicted to encode a polypeptide of 346 amino acid residues with a deduced molecular mass of 41 455 Da. No homology with any previously described genes was found. A probe was used to determine the presence of this gene in two strains on 31 tested.
+A gene which encodes resistance by abortive infection (Abi+) to bacteriophage was cloned from Lactococcus lactis ssp. lactis biovar. diacetylactis S94. This gene was found to confer a reduction in efficiency of plating and plaque size for prolate-headed bacteriophage phi 53 (group I of homology) and total resistance to the small isometric-headed bacteriophage phi 59 (group III of homology). The cloned gene is predicted to encode a polypeptide of 346 amino acid residues with a deduced molecular mass of 41 455 Da. No homology with any previously described genes was found. A probe was used to determine the presence of this gene in two strains on 31 tested.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiH
 ## Example of genomic structure
 
 The AbiH system is composed of one protein: AbiH.
diff --git a/content/2.defense-systems/abii.md b/content/2.defense-systems/abii.md
index a53e4fc086e782068cfb3db899826efc4c32b338..3878ce0e99c5681b6865050033aeb316eb36f877 100644
--- a/content/2.defense-systems/abii.md
+++ b/content/2.defense-systems/abii.md
@@ -1,7 +1,16 @@
 ---
 title: AbiI
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiI
 ## Example of genomic structure
 
 The AbiI system is composed of one protein: AbiI.
diff --git a/content/2.defense-systems/abij.md b/content/2.defense-systems/abij.md
index 449c1f8edad6e8a70ea322ff37d82972a410d862..36cfb76c321ea911ec95f35bc3ecbad7d48b2df8 100644
--- a/content/2.defense-systems/abij.md
+++ b/content/2.defense-systems/abij.md
@@ -1,7 +1,16 @@
 ---
 title: AbiJ
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiJ
 ## Example of genomic structure
 
 The AbiJ system is composed of one protein: AbiJ.
diff --git a/content/2.defense-systems/abik.md b/content/2.defense-systems/abik.md
index 95064f3a1752cc45fcbb645f1e4a20704c7cc557..963d4af61257da4bdfce303e9416f6a2a1c725cf 100644
--- a/content/2.defense-systems/abik.md
+++ b/content/2.defense-systems/abik.md
@@ -1,7 +1,16 @@
 ---
 title: AbiK
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiK
 ## Example of genomic structure
 
 The AbiK system is composed of one protein: AbiK.
diff --git a/content/2.defense-systems/abil.md b/content/2.defense-systems/abil.md
index a430cc78a207a150e8e4a7ec095a492aede4357c..d3a79a533c16ac2dd58ea8f4d6b8614a3e27be52 100644
--- a/content/2.defense-systems/abil.md
+++ b/content/2.defense-systems/abil.md
@@ -1,7 +1,16 @@
 ---
 title: AbiL
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiL
 ## Example of genomic structure
 
 The AbiL system is composed of 2 proteins: AbiLii2 and, AbiLi2.
diff --git a/content/2.defense-systems/abin.md b/content/2.defense-systems/abin.md
index 8bf8cc5d3dda9483a8a0d125fec5a0bc060aceed..8a5f7395917756693186769d4c0a50019ed0b20d 100644
--- a/content/2.defense-systems/abin.md
+++ b/content/2.defense-systems/abin.md
@@ -1,7 +1,16 @@
 ---
 title: AbiN
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiN
 ## Example of genomic structure
 
 The AbiN system is composed of one protein: AbiN.
diff --git a/content/2.defense-systems/abio.md b/content/2.defense-systems/abio.md
index e7e1d1712e70091b12fe605e5a1fa818acc53594..3929456acc4cefdb10eaf588c2c9b08c3f0d8ca1 100644
--- a/content/2.defense-systems/abio.md
+++ b/content/2.defense-systems/abio.md
@@ -1,7 +1,16 @@
 ---
 title: AbiO
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiO
 ## Example of genomic structure
 
 The AbiO system is composed of one protein: AbiO.
diff --git a/content/2.defense-systems/abip2.md b/content/2.defense-systems/abip2.md
index d27812ac410f642f71d9d914999868934c8baae2..27347c2d3f25cca0959348025fbc585c9094fe67 100644
--- a/content/2.defense-systems/abip2.md
+++ b/content/2.defense-systems/abip2.md
@@ -1,7 +1,16 @@
 ---
 title: AbiP2
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiP2
 ## Example of genomic structure
 
 The AbiP2 system is composed of one protein: AbiP2.
diff --git a/content/2.defense-systems/abiq.md b/content/2.defense-systems/abiq.md
index f676d709b69b602e95d9cf6a079102e12386c7f2..545fb310d65ef34df8b413904da2e1ae3e1561de 100644
--- a/content/2.defense-systems/abiq.md
+++ b/content/2.defense-systems/abiq.md
@@ -1,7 +1,16 @@
 ---
 title: AbiQ
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiQ
 ## Example of genomic structure
 
 The AbiQ system is composed of one protein: AbiQ.
diff --git a/content/2.defense-systems/abir.md b/content/2.defense-systems/abir.md
index a20e293edf0adf675aabf8fc2e1bf7109789524a..c4faa2091fe461eaedef6d381fbd918b0659e3eb 100644
--- a/content/2.defense-systems/abir.md
+++ b/content/2.defense-systems/abir.md
@@ -1,7 +1,16 @@
 ---
 title: AbiR
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiR
 ## Example of genomic structure
 
 The AbiR system is composed of 3 proteins: AbiRc, AbiRb and, AbiRa.
diff --git a/content/2.defense-systems/abit.md b/content/2.defense-systems/abit.md
index f5ed6e477d6826ad71a2dc9148dac4dfdcb1654c..310f1bdef51037b8647d0fb5b1f7c367255185c5 100644
--- a/content/2.defense-systems/abit.md
+++ b/content/2.defense-systems/abit.md
@@ -1,7 +1,16 @@
 ---
 title: AbiT
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiT
 ## Example of genomic structure
 
 The AbiT system is composed of 2 proteins: AbiTii and, AbiTi.
diff --git a/content/2.defense-systems/abiu.md b/content/2.defense-systems/abiu.md
index 3fe09695443021d7f0ec7931c64421478bced0fb..319cf7e8503ce06adfc0a76603391b60a8ce44af 100644
--- a/content/2.defense-systems/abiu.md
+++ b/content/2.defense-systems/abiu.md
@@ -1,7 +1,16 @@
 ---
 title: AbiU
+tableColumns:
+    article:
+      doi: 10.1016/j.mib.2005.06.006
+      abstract: |
+Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiU
 ## Example of genomic structure
 
 The AbiU system is composed of one protein: AbiU.
diff --git a/content/2.defense-systems/abiv.md b/content/2.defense-systems/abiv.md
index c9a67d7fe5cfcff60c88c91293543878d0a1e4d9..3734e7e908a7f4f21b28ae0afb46048d499ef1dc 100644
--- a/content/2.defense-systems/abiv.md
+++ b/content/2.defense-systems/abiv.md
@@ -3,8 +3,14 @@ title: AbiV
 tableColumns:
     article:
       doi: 10.1128/AEM.00780-08
+      abstract: |
+Insertional mutagenesis with pGhost9::ISS1 resulted in independent insertions in a 350-bp region of the chromosome of Lactococcus lactis subsp. cremoris MG1363 that conferred phage resistance to the integrants. The orientation and location of the insertions suggested that the phage resistance phenotype was caused by a chromosomal gene turned on by a promoter from the inserted construct. Reverse transcription-PCR analysis confirmed that there were higher levels of transcription of a downstream open reading frame (ORF) in the phage-resistant integrants than in the phage-sensitive strain L. lactis MG1363. This gene was also found to confer phage resistance to L. lactis MG1363 when it was cloned into an expression vector. A subsequent frameshift mutation in the ORF completely eliminated the phage resistance phenotype, confirming that the ORF was necessary for phage resistance. This ORF provided resistance against virulent lactococcal phages belonging to the 936 and c2 species with an efficiency of plaquing of 10?4, but it did not protect against members of the P335 species. A high level of expression of the ORF did not affect the cellular growth rate. Assays for phage adsorption, DNA ejection, restriction/modification activity, plaque size, phage DNA replication, and cell survival showed that the ORF encoded an abortive infection (Abi) mechanism. Sequence analysis revealed a deduced protein consisting of 201 amino acids which, in its native state, probably forms a dimer in the cytosol. Similarity searches revealed no homology to other phage resistance mechanisms, and thus, this novel Abi mechanism was designated AbiV. The mode of action of AbiV is unknown, but the activity of AbiV prevented cleavage of the replicated phage DNA of 936-like phages.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# AbiV
 ## Example of genomic structure
 
 The AbiV system is composed of one protein: AbiV.
diff --git a/content/2.defense-systems/abiz.md b/content/2.defense-systems/abiz.md
index f82e3574793c1db1f164e1820be492ab68c0ec05..f36bce224032937e1d73fe7221341acf410f9f99 100644
--- a/content/2.defense-systems/abiz.md
+++ b/content/2.defense-systems/abiz.md
@@ -1,7 +1,16 @@
 ---
 title: AbiZ
+tableColumns:
+    article:
+      doi: 10.1128/JB.00904-06
+      abstract: |
+The conjugative plasmid pTR2030 has been used extensively to confer phage resistance in commercial Lactococcus starter cultures. The plasmid harbors a 16-kb region, flanked by insertion sequence (IS) elements, that encodes the restriction/modification system LlaI and carries an abortive infection gene, abiA. The AbiA system inhibits both prolate and small isometric phages by interfering with the early stages of phage DNA replication. However, abiA alone does not account for the full abortive activity reported for pTR2030. In this study, a 7.5-kb region positioned within the IS elements and downstream of abiA was sequenced to reveal seven additional open reading frames (ORFs). A single ORF, designated abiZ, was found to be responsible for a significant reduction in plaque size and an efficiency of plaquing (EOP) of 10?6, without affecting phage adsorption. AbiZ causes phage ?31-infected Lactococcus lactis NCK203 to lyse 15 min early, reducing the burst size of ?31 100-fold. Thirteen of 14 phages of the P335 group were sensitive to AbiZ, through reduction in either plaque size, EOP, or both. The predicted AbiZ protein contains two predicted transmembrane helices but shows no significant DNA homologies. When the phage ?31 lysin and holin genes were cloned into the nisin-inducible shuttle vector pMSP3545, nisin induction of holin and lysin caused partial lysis of NCK203. In the presence of AbiZ, lysis occurred 30 min earlier. In holin-induced cells, membrane permeability as measured using propidium iodide was greater in the presence of AbiZ. These results suggest that AbiZ may interact cooperatively with holin to cause premature lysis.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Membrane disrupting
 ---
 
+# AbiZ
 ## Example of genomic structure
 
 The AbiZ system is composed of one protein: AbiZ.
diff --git a/content/2.defense-systems/aditi.md b/content/2.defense-systems/aditi.md
index 090a5eb4256387dcaf15ff413dcf9b57618b7065..0889597f050291cc61d017590fd1959df8ecb7fc 100644
--- a/content/2.defense-systems/aditi.md
+++ b/content/2.defense-systems/aditi.md
@@ -1,7 +1,16 @@
 ---
 title: Aditi
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Aditi
 ## Example of genomic structure
 
 The Aditi system is composed of 2 proteins: DitB and, DitA.
diff --git a/content/2.defense-systems/avast.md b/content/2.defense-systems/avast.md
index 2bc639dc64ba6c108272ea3cbbb1a2a3fa68d960..ea396403e872d31ad594f095697d3fb53c8f5077 100644
--- a/content/2.defense-systems/avast.md
+++ b/content/2.defense-systems/avast.md
@@ -1,7 +1,17 @@
 ---
 title: AVAST
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Sensing of phage protein
+    Activator: Direct binding
+    Effector: Diverse effectors (Nucleic acid degrading, putative Nucleotide modifying, putative Membrane disrupting)
+
 ---
 
+# AVAST
 ## Description 
 AVAST (antiviral ATPases/NTPases of the STAND superfamily) is a group of anti-phage defense systems, active against some dsDNA phages. 
 
diff --git a/content/2.defense-systems/azaca.md b/content/2.defense-systems/azaca.md
index bdf5238f6798571889c94797fc02f4f74744c8b8..c804b46c7a89c6b68b62c1a7d67a260116af76a9 100644
--- a/content/2.defense-systems/azaca.md
+++ b/content/2.defense-systems/azaca.md
@@ -1,7 +1,16 @@
 ---
 title: Azaca
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Azaca
 ## Example of genomic structure
 
 The Azaca system is composed of 3 proteins: ZacA, ZacB and, ZacC.
diff --git a/content/2.defense-systems/borvo.md b/content/2.defense-systems/borvo.md
index 25ac50d7cced68a19a8374da94cd626df614c998..6f8d3bddb1983f63bfc060bfa3aad6b5e8b5d963 100644
--- a/content/2.defense-systems/borvo.md
+++ b/content/2.defense-systems/borvo.md
@@ -1,7 +1,16 @@
 ---
 title: Borvo
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Borvo
 ## Example of genomic structure
 
 The Borvo system is composed of one protein: BovA.
diff --git a/content/2.defense-systems/brex.md b/content/2.defense-systems/brex.md
index 6444013cdd02c003e15eade51e7abecb52aa7653..2ed1eaa0192128931a0ef6eb37932ee2906b2051 100644
--- a/content/2.defense-systems/brex.md
+++ b/content/2.defense-systems/brex.md
@@ -1,7 +1,16 @@
 ---
 title: BREX
+tableColumns:
+    article:
+      doi: 10.15252/embj.201489455
+      abstract: |
+The perpetual arms race between bacteria and phage has resulted in the evolution of efficient resistance systems that protect bacteria from phage infection. Such systems, which include the CRISPR-Cas and restriction-modification systems, have proven to be invaluable in the biotechnology and dairy industries. Here, we report on a six-gene cassette in Bacillus cereus which, when integrated into the Bacillus subtilis genome, confers resistance to a broad range of phages, including both virulent and temperate ones. This cassette includes a putative Lon-like protease, an alkaline phosphatase domain protein, a putative RNA-binding protein, a DNA methylase, an ATPase-domain protein, and a protein of unknown function. We denote this novel defense system BREX (Bacteriophage Exclusion) and show that it allows phage adsorption but blocks phage DNA replication. Furthermore, our results suggest that methylation on non-palindromic TAGGAG motifs in the bacterial genome guides self/non-self discrimination and is essential for the defensive function of the BREX system. However, unlike restriction-modification systems, phage DNA does not appear to be cleaved or degraded by BREX, suggesting a novel mechanism of defense. Pan genomic analysis revealed that BREX and BREX-like systems, including the distantly related Pgl system described in Streptomyces coelicolor, are widely distributed in ~10% of all sequenced microbial genomes and can be divided into six coherent subtypes in which the gene composition and order is conserved. Finally, we detected a phage family that evades the BREX defense, implying that anti-BREX mechanisms may have evolved in some phages as part of their arms race with bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# BREX
 ## Description
 
 BREX (for Bacteriophage Exclusion) is a family of anti-phage defense systems. BREX systems are active against both lytic and lysogenic phages. They allow phage adsorption but block phage DNA replication, and are considered to be [RM](/defense-systems/rm)-like systems (1,2). BREX systems are found in around 10% of sequenced microbial genomes (1).
diff --git a/content/2.defense-systems/bsta.md b/content/2.defense-systems/bsta.md
index bf04f9f667b32fcb6a0c8fe829116480490cae03..dc6a4842bab400b0878be715cbd626bd137e530b 100644
--- a/content/2.defense-systems/bsta.md
+++ b/content/2.defense-systems/bsta.md
@@ -1,7 +1,16 @@
 ---
 title: BstA
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2021.09.002
+      abstract: |
+Temperate phages are pervasive in bacterial genomes, existing as vertically inherited islands termed prophages. Prophages are vulnerable to predation of their host bacterium by exogenous phages. Here, we identify BstA, a family of prophage-encoded phage-defense proteins in diverse Gram-negative bacteria. BstA localizes to sites of exogenous phage DNA replication and mediates abortive infection, suppressing the competing phage epidemic. During lytic replication, the BstA-encoding prophage is not itself inhibited by BstA due to self-immunity conferred by the anti-BstA (aba) element, a short stretch of DNA within the bstA locus. Inhibition of phage replication by distinct BstA proteins from Salmonella, Klebsiella, and Escherichia prophages is generally interchangeable, but each possesses a cognate aba element. The specificity of the aba element ensures that immunity is exclusive to the replicating prophage, preventing exploitation by variant BstA-encoding phages. The BstA protein allows prophages to defend host cells against exogenous phage attack without sacrificing the ability to replicate lytically.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# BstA
 ## Description
 
 BstA is a family of defense systems. BtsA systems from *Salmonella enterica subsp. enterica*, *Klebsiella pneumoniae* and *Escherichia coli* have been shown to provide resistance against a large diversity of phages when expressed in a *S. enterica* or *E.coli* host (1).
diff --git a/content/2.defense-systems/bunzi.md b/content/2.defense-systems/bunzi.md
index 6986429c90118e459fa5d4e80157bb717ec329cb..ae2464b4889eb99ffaf32747a1064705cae34b1c 100644
--- a/content/2.defense-systems/bunzi.md
+++ b/content/2.defense-systems/bunzi.md
@@ -1,7 +1,16 @@
 ---
 title: Bunzi
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Bunzi
 ## Example of genomic structure
 
 The Bunzi system is composed of 2 proteins: BnzB and, BnzA.
diff --git a/content/2.defense-systems/caprel.md b/content/2.defense-systems/caprel.md
index 8c35327d19d970e3c4878dea2b6ebfba77cfc5fb..c89b53b20878f53f73a8e776196364a37d1b4dc5 100644
--- a/content/2.defense-systems/caprel.md
+++ b/content/2.defense-systems/caprel.md
@@ -1,7 +1,16 @@
 ---
 title: CapRel
+tableColumns:
+    article:
+      doi: 10.1038/s41586-022-05444-z
+      abstract: |
+Bacteria have evolved diverse immunity mechanisms to protect themselves against the constant onslaught of bacteriophages1–3. Similar to how eukaryotic innate immune systems sense foreign invaders through pathogen-associated molecular patterns4 (PAMPs), many bacterial immune systems that respond to bacteriophage infection require phage-specific triggers to be activated. However, the identities of such triggers and the sensing mechanisms remain largely unknown. Here we identify and investigate the anti-phage function of CapRelSJ46, a fused toxin–antitoxin system that protects Escherichia coli against diverse phages. Using genetic, biochemical and structural analyses, we demonstrate that the C-terminal domain of CapRelSJ46 regulates the toxic N-terminal region, serving as both antitoxin and phage infection sensor. Following infection by certain phages, newly synthesized major capsid protein binds directly to the C-terminal domain of CapRelSJ46 to relieve autoinhibition, enabling the toxin domain to pyrophosphorylate tRNAs, which blocks translation to restrict viral infection. Collectively, our results reveal the molecular mechanism by which a bacterial immune system directly senses a conserved, essential component of phages, suggesting a PAMP-like sensing model for toxin–antitoxin-mediated innate immunity in bacteria. We provide evidence that CapRels and their phage-encoded triggers are engaged in a ‘Red Queen conflict’5, revealing a new front in the intense coevolutionary battle between phages and bacteria. Given that capsid proteins of some eukaryotic viruses are known to stimulate innate immune signalling in mammalian hosts6–10, our results reveal a deeply conserved facet of immunity.
+    Sensor: Sensing of phage protein
+    Activator: Direct
+    Effector: Nucleic acid degrading (pyrophosphorylates tRNAs)
 ---
 
+# CapRel
 ## Description
 
 CapRel is a fused toxin–antitoxin system that is active against diverse phages when expressed in *Escherichia coli*. CapRel belongs to the family of toxSAS toxin–antitoxin systems. CapRel is an Abortive infection system which is found in Cyanobacteria, Actinobacteria, and Proteobacteria, Spirochetes, Bacteroidetes, and Firmicutes, as well as in some temperate phages.
diff --git a/content/2.defense-systems/cbass.md b/content/2.defense-systems/cbass.md
index 8d61883581faf2268b39e618dbec0158dcfbd44c..03681e23f535131de296a7fda978356a07402156 100644
--- a/content/2.defense-systems/cbass.md
+++ b/content/2.defense-systems/cbass.md
@@ -1,7 +1,16 @@
 ---
 title: CBASS
+tableColumns:
+    article:
+      doi: 10.1038/s41564-020-0777-y
+      abstract: |
+Cyclic-oligonucleotide-based anti-phage signalling systems (CBASS) are a family of defence systems against bacteriophages (hereafter phages) that share ancestry with the cGAS–STING innate immune pathway in animals. CBASS systems are composed of an oligonucleotide cyclase, which generates signalling cyclic oligonucleotides in response to phage infection, and an effector that is activated by the cyclic oligonucleotides and promotes cell death. Cell death occurs before phage replication is completed, therefore preventing the spread of phages to nearby cells. Here, we analysed 38,000 bacterial and archaeal genomes and identified more than 5,000 CBASS systems, which have diverse architectures with multiple signalling molecules, effectors and ancillary genes. We propose a classification system for CBASS that groups systems according to their operon organization, signalling molecules and effector function. Four major CBASS types were identified, sharing at least six effector subtypes that promote cell death by membrane impairment, DNA degradation or other means. We observed evidence of extensive gain and loss of CBASS systems, as well as shuffling of effector genes between systems. We expect that our classification and nomenclature scheme will guide future research in the developing CBASS field.
+    Sensor: Unknown
+    Activator: Signaling molecules
+    Effector: Divers (Nucleic acid degrading, Nucleotide modifying, Membrane disrupting)
 ---
 
+# CBASS
 ## Example of genomic structure
 
 The CBASS system have been describe in a total of 5 subsystems.
diff --git a/content/2.defense-systems/dartg.md b/content/2.defense-systems/dartg.md
index 5b45549d9ea1f2cdc9ac843364c3960d94c48f5b..24d1aa4b8d7d6dd3a30373c27f08c0ec86d5e4ba 100644
--- a/content/2.defense-systems/dartg.md
+++ b/content/2.defense-systems/dartg.md
@@ -1,7 +1,16 @@
 ---
 title: DarTG
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01153-5
+      abstract: |
+Toxin-antitoxin (TA) systems are broadly distributed, yet poorly conserved, genetic elements whose biological functions are unclear and controversial. Some TA systems may provide bacteria with immunity to infection by their ubiquitous viral predators, bacteriophages. To identify such TA systems, we searched bioinformatically for those frequently encoded near known phage defence genes in bacterial genomes. This search identified homologues of DarTG, a recently discovered family of TA systems whose biological functions and natural activating conditions were unclear. Representatives from two different subfamilies, DarTG1 and DarTG2, strongly protected E. coli MG1655 against different phages. We demonstrate that for each system, infection with either RB69 or T5 phage, respectively, triggers release of the DarT toxin, a DNA ADP-ribosyltransferase, that then modifies viral DNA and prevents replication, thereby blocking the production of mature virions. Further, we isolated phages that have evolved to overcome DarTG defence either through mutations to their DNA polymerase or to an anti-DarT factor, gp61.2, encoded by many T-even phages. Collectively, our results indicate that phage defence may be a common function for TA systems and reveal the mechanism by which DarTG systems inhibit phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Nucleic acid degrading (ADP-ribosylation)
 ---
 
+# DarTG
 ## Example of genomic structure
 
 The DarTG system is composed of 2 proteins: DarT and, DarG.
diff --git a/content/2.defense-systems/dazbog.md b/content/2.defense-systems/dazbog.md
index d76dbf5d1758a3b1c4ac1d0dfe67026e8de146de..b5176aaeea528ac39a18452d79535d10067a0ba8 100644
--- a/content/2.defense-systems/dazbog.md
+++ b/content/2.defense-systems/dazbog.md
@@ -1,7 +1,16 @@
 ---
 title: Dazbog
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Dazbog
 ## Example of genomic structure
 
 The Dazbog system is composed of 2 proteins: DzbB and, DzbA.
diff --git a/content/2.defense-systems/dctpdeaminase.md b/content/2.defense-systems/dctpdeaminase.md
index cd52ecd7ff2cbf7789399aa6e9f5f02ff0a5517b..374128bf7e04411d1f502e5fa9ea76384d8f64fa 100644
--- a/content/2.defense-systems/dctpdeaminase.md
+++ b/content/2.defense-systems/dctpdeaminase.md
@@ -1,7 +1,16 @@
 ---
 title: dCTPdeaminase
+tableColumns:
+    article:
+      doi: 10.1016/j.cell.2021.09.031
+      abstract: |
+The cyclic pyrimidines 3',5'-cyclic cytidine monophosphate (cCMP) and 3',5'-cyclic uridine monophosphate (cUMP) have been reported in multiple organisms and cell types. As opposed to the cyclic nucleotides 3',5'-cyclic adenosine monophosphate (cAMP) and 3',5'-cyclic guanosine monophosphate (cGMP), which are second messenger molecules with well-established regulatory roles across all domains of life, the biological role of cyclic pyrimidines has remained unclear. Here we report that cCMP and cUMP are second messengers functioning in bacterial immunity against viruses. We discovered a family of bacterial pyrimidine cyclase enzymes that specifically synthesize cCMP and cUMP following phage infection and demonstrate that these molecules activate immune effectors that execute an antiviral response. A crystal structure of a uridylate cyclase enzyme from this family explains the molecular mechanism of selectivity for pyrimidines as cyclization substrates. Defense systems encoding pyrimidine cyclases, denoted here Pycsar (pyrimidine cyclase system for antiphage resistance), are widespread in prokaryotes. Our results assign clear biological function to cCMP and cUMP as immunity signaling molecules in bacteria.
+    Sensor: Monitoring of the host cell machinery integrity
+    Activator: Direct
+    Effector: Nucleotide modifying
 ---
 
+# dCTPdeaminase
 ## Description
 dCTPdeaminase is a family of systems. dCTPdeaminase from Escherichia coli has been shown to provide resistance against various lytic phages when express heterologously in another Escherichia coli.
 This system is mostly found in Proteobacteria but a few examples also exist in Acidobacteria, Actinobacteria, Bacteroidetes, Cyanobacteria, Firmicutes, Planctomyces, and Verrucomicrobia.
diff --git a/content/2.defense-systems/dgtpase.md b/content/2.defense-systems/dgtpase.md
index 66546b6a341974f7b48802e85a63879fc3c677eb..e95bc4401f780300128eef82217e899fc729ad30 100644
--- a/content/2.defense-systems/dgtpase.md
+++ b/content/2.defense-systems/dgtpase.md
@@ -1,9 +1,17 @@
 ---
 title: dGTPase
----
-title: dGTPase
+tableColumns:
+    article:
+      doi: 10.1016/j.cell.2021.09.031
+      abstract: |
+The cyclic pyrimidines 3',5'-cyclic cytidine monophosphate (cCMP) and 3',5'-cyclic uridine monophosphate (cUMP) have been reported in multiple organisms and cell types. As opposed to the cyclic nucleotides 3',5'-cyclic adenosine monophosphate (cAMP) and 3',5'-cyclic guanosine monophosphate (cGMP), which are second messenger molecules with well-established regulatory roles across all domains of life, the biological role of cyclic pyrimidines has remained unclear. Here we report that cCMP and cUMP are second messengers functioning in bacterial immunity against viruses. We discovered a family of bacterial pyrimidine cyclase enzymes that specifically synthesize cCMP and cUMP following phage infection and demonstrate that these molecules activate immune effectors that execute an antiviral response. A crystal structure of a uridylate cyclase enzyme from this family explains the molecular mechanism of selectivity for pyrimidines as cyclization substrates. Defense systems encoding pyrimidine cyclases, denoted here Pycsar (pyrimidine cyclase system for antiphage resistance), are widespread in prokaryotes. Our results assign clear biological function to cCMP and cUMP as immunity signaling molecules in bacteria.
+    Sensor: Monitoring of the host cell machinery integrity
+    Activator: Direc
+    Effector: Nucleotide modifying
 ---
 
+# dGTPase
+# dGTPase
 ## Example of genomic structure
 
 The dGTPase system is composed of one protein: Sp_dGTPase.
diff --git a/content/2.defense-systems/disarm.md b/content/2.defense-systems/disarm.md
index 54bf34512be2700fc68d4cf83512a42430af3395..9c776353cd1a63ffa2fb7cf08372c9ef63cbdb70 100644
--- a/content/2.defense-systems/disarm.md
+++ b/content/2.defense-systems/disarm.md
@@ -1,7 +1,16 @@
 ---
 title: DISARM
+tableColumns:
+    article:
+      doi: 10.1038/s41564-017-0051-0
+      abstract: |
+The evolutionary pressure imposed by phage predation on bacteria and archaea has resulted in the development of effective anti-phage defence mechanisms, including restriction–modification and CRISPR–Cas systems. Here, we report on a new defence system, DISARM (defence island system associated with restriction–modification), which is widespread in bacteria and archaea. DISARM is composed of five genes, including a DNA methylase and four other genes annotated as a helicase domain, a phospholipase D (PLD) domain, a DUF1998 domain and a gene of unknown function. Engineering the Bacillus paralicheniformis 9945a DISARM system into Bacillus subtilis has rendered the engineered bacteria protected against phages from all three major families of tailed double-stranded DNA phages. Using a series of gene deletions, we show that four of the five genes are essential for DISARM-mediated defence, with the fifth (PLD) being redundant for defence against some of the phages. We further show that DISARM restricts incoming phage DNA and that the B. paralicheniformis DISARM methylase modifies host CCWGG motifs as a marker of self DNA akin to restriction–modification systems. Our results suggest that DISARM is a new type of multi-gene restriction–modification module, expanding the arsenal of defence systems known to be at the disposal of prokaryotes against their viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# DISARM
 ## Description
 
 DISARM (Defense Island System Associated with Restriction-Modification) is a defense system widespread in prokaryotes, encoded by a 5-gene cassette. DISARM provides broad protection against double-stranded DNA phages, including siphophages, myophages, and podophages (1,3).
diff --git a/content/2.defense-systems/dmdde.md b/content/2.defense-systems/dmdde.md
index e4b676e97f3b585499c27f82958183a30c3a4d36..22e3900636e62e3ce2818026693240ee436d3123 100644
--- a/content/2.defense-systems/dmdde.md
+++ b/content/2.defense-systems/dmdde.md
@@ -1,7 +1,13 @@
 ---
 title: DmdDE
+tableColumns:
+    article:
+      doi: 10.1038/s41586-022-04546-y
+      abstract: |
+Horizontal gene transfer can trigger rapid shifts in bacterial evolution. Driven by a variety of mobile genetic elements—in particular bacteriophages and plasmids—the ability to share genes within and across species underpins the exceptional adaptability of bacteria. Nevertheless, invasive mobile genetic elements can also present grave risks to the host; bacteria have therefore evolved a vast array of defences against these elements1. Here we identify two plasmid defence systems conserved in the Vibrio cholerae El Tor strains responsible for the ongoing seventh cholera pandemic2–4. These systems, termed DdmABC and DdmDE, are encoded on two major pathogenicity islands that are a hallmark of current pandemic strains. We show that the modules cooperate to rapidly eliminate small multicopy plasmids by degradation. Moreover, the DdmABC system is widespread and can defend against bacteriophage infection by triggering cell suicide (abortive infection, or Abi). Notably, we go on to show that, through an Abi-like mechanism, DdmABC increases the burden of large low-copy-number conjugative plasmids, including a broad-host IncC multidrug resistance plasmid, which creates a fitness disadvantage that counterselects against plasmid-carrying cells. Our results answer the long-standing question of why plasmids, although abundant in environmental strains, are rare in pandemic strains; have implications for understanding the dissemination of antibiotic resistance plasmids; and provide insights into how the interplay between two defence systems has shaped the evolution of the most successful lineage of pandemic V. cholerae.
 ---
 
+# DmdDE
 ## Example of genomic structure
 
 The DmdDE system is composed of 2 proteins: DdmE and, DdmD.
diff --git a/content/2.defense-systems/dnd.md b/content/2.defense-systems/dnd.md
index 9d7a139aa2237a7d3f689cd1ebf10ddb4a7aa318..06b7d537b6a68748166ac571bd71bacfa33136a3 100644
--- a/content/2.defense-systems/dnd.md
+++ b/content/2.defense-systems/dnd.md
@@ -1,7 +1,16 @@
 ---
 title: Dnd
+tableColumns:
+    article:
+      doi: 10.1038/nchembio.2007.39
+      abstract: |
+Modifications of the canonical structures of DNA and RNA play critical roles in cell physiology, DNA replication, transcription and translation in all organisms. We now report that bacterial dnd gene clusters incorporate sulfur into the DNA backbone as a sequence-selective, stereospecific phosphorothioate modification. To our knowledge, unlike any other DNA or RNA modification systems, DNA phosphorothioation by dnd gene clusters is the first physiological modification described on the DNA backbone.
+    Sensor: Detecting invading nucleic acid
+    Activator: Unknown
+    Effector: Nucleic acid degrading
 ---
 
+# Dnd
 ## Example of genomic structure
 
 The Dnd system have been describe in a total of 2 subsystems.
diff --git a/content/2.defense-systems/dodola.md b/content/2.defense-systems/dodola.md
index f6eb30da0cdebe7dee4ae66d1105126d0c76c38c..7f849fd3eab2aa729bc377a51e448b88fc504e54 100644
--- a/content/2.defense-systems/dodola.md
+++ b/content/2.defense-systems/dodola.md
@@ -1,7 +1,16 @@
 ---
 title: Dodola
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Dodola
 ## Example of genomic structure
 
 The Dodola system is composed of 2 proteins: DolA and, DolB.
diff --git a/content/2.defense-systems/dpd.md b/content/2.defense-systems/dpd.md
index cd598667fda90add8525e86f5c614fd3ad9260c4..a464989dc467acf652bdec429ff254b063d063e4 100644
--- a/content/2.defense-systems/dpd.md
+++ b/content/2.defense-systems/dpd.md
@@ -1,7 +1,13 @@
 ---
 title: Dpd
+tableColumns:
+    article:
+      doi: 10.1073/pnas.1518570113
+      abstract: |
+The discovery of ?20-kb gene clusters containing a family of paralogs of tRNA guanosine transglycosylase genes, called tgtA5, alongside 7-cyano-7-deazaguanine (preQ0) synthesis and DNA metabolism genes, led to the hypothesis that 7-deazaguanine derivatives are inserted in DNA. This was established by detecting 2’-deoxy-preQ0 and 2’-deoxy-7-amido-7-deazaguanosine in enzymatic hydrolysates of DNA extracted from the pathogenic, Gram-negative bacteria Salmonella enterica serovar Montevideo. These modifications were absent in the closely related S. enterica serovar Typhimurium LT2 and from a mutant of S. Montevideo, each lacking the gene cluster. This led us to rename the genes of the S. Montevideo cluster as dpdA-K for 7-deazapurine in DNA. Similar gene clusters were analyzed in ?150 phylogenetically diverse bacteria, and the modifications were detected in DNA from other organisms containing these clusters, including Kineococcus radiotolerans, Comamonas testosteroni, and Sphingopyxis alaskensis. Comparative genomic analysis shows that, in Enterobacteriaceae, the cluster is a genomic island integrated at the leuX locus, and the phylogenetic analysis of the TgtA5 family is consistent with widespread horizontal gene transfer. Comparison of transformation efficiencies of modified or unmodified plasmids into isogenic S. Montevideo strains containing or lacking the cluster strongly suggests a restriction–modification role for the cluster in Enterobacteriaceae. Another preQ0 derivative, 2’-deoxy-7-formamidino-7-deazaguanosine, was found in the Escherichia coli bacteriophage 9g, as predicted from the presence of homologs of genes involved in the synthesis of the archaeosine tRNA modification. These results illustrate a deep and unexpected evolutionary connection between DNA and tRNA metabolism.
 ---
 
+# Dpd
 ## Example of genomic structure
 
 The Dpd system is composed of 15 proteins: FolE, QueD, DpdC, DpdA, DpdB, QueC, DpdD, DpdK, DpdJ, DpdI, DpdH, DpdG, DpdF, DpdE and, QueE.
diff --git a/content/2.defense-systems/drt.md b/content/2.defense-systems/drt.md
index 4ca1ebb306862b9b0d7b0cb5888662151bff7946..36f81edb18cd864149771a27c05fd8559f4bf5d5 100644
--- a/content/2.defense-systems/drt.md
+++ b/content/2.defense-systems/drt.md
@@ -1,7 +1,16 @@
 ---
 title: DRT
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# DRT
 ## Example of genomic structure
 
 The DRT system have been describe in a total of 9 subsystems.
diff --git a/content/2.defense-systems/druantia.md b/content/2.defense-systems/druantia.md
index 901cc9d93b088d1c414dba1ff04be9bfc98f512c..4a917bf38573baa346fb2dd664bbf15a48ccb46c 100644
--- a/content/2.defense-systems/druantia.md
+++ b/content/2.defense-systems/druantia.md
@@ -1,7 +1,16 @@
 ---
 title: Druantia
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Druantia
 ## Example of genomic structure
 
 The Druantia system have been describe in a total of 3 subsystems.
diff --git a/content/2.defense-systems/dsr.md b/content/2.defense-systems/dsr.md
index b8294e7a7b1c300b54ed11367a083f1d85f0e2fb..6e1bf3cf9b9f6e881bfcf5b1615e477fbc8c0834 100644
--- a/content/2.defense-systems/dsr.md
+++ b/content/2.defense-systems/dsr.md
@@ -1,7 +1,16 @@
 ---
 title: Dsr
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Sensing phage protein
+    Activator: Direct
+    Effector: Nucleotide modifying
 ---
 
+# Dsr
 ## Example of genomic structure
 
 The Dsr system have been describe in a total of 2 subsystems.
diff --git a/content/2.defense-systems/eleos.md b/content/2.defense-systems/eleos.md
index c1664f0d25766a11811f233b048ccfdd1dfb8fa2..2f8e1ef475ba90b583998f96415e23c17b241303 100644
--- a/content/2.defense-systems/eleos.md
+++ b/content/2.defense-systems/eleos.md
@@ -1,7 +1,16 @@
 ---
 title: Eleos
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Eleos
 The Eleos system was previously described as the Dynamins-like system in (Millman et al, 2022).
 
 ## Example of genomic structure
diff --git a/content/2.defense-systems/gabija.md b/content/2.defense-systems/gabija.md
index ec4d44eec170e6c79a53d17b15241d4c2fa33b70..1157ad7d72ff95fb406d54f4297fa548b5b0b514 100644
--- a/content/2.defense-systems/gabija.md
+++ b/content/2.defense-systems/gabija.md
@@ -1,7 +1,16 @@
 ---
 title: Gabija
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Direct
+    Effector: Degrading nucleic acids
 ---
 
+# Gabija
 ## Description
 
 According to recent studies, GajA is a sequence-specific DNA nicking endonuclease, whose activity is inhibited by nucleotide concentration. Accordingly, GajA would be fully inhibited at cellular nucleotides concentrations. It was hypothesized that upon nucleotide depletion during phage infection, GajA would become activated (2). 
diff --git a/content/2.defense-systems/gao_ape.md b/content/2.defense-systems/gao_ape.md
index 41e8bec7fff51c307c6abdfcfb2278530f578c59..ce9829f5f1a9f3cd924100dacd282ac8bfaac321 100644
--- a/content/2.defense-systems/gao_ape.md
+++ b/content/2.defense-systems/gao_ape.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Ape
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Ape
 ## Example of genomic structure
 
 The Gao_Ape system is composed of one protein: ApeA.
diff --git a/content/2.defense-systems/gao_her.md b/content/2.defense-systems/gao_her.md
index 9c2c8906bc16bed72aff43ff79af2259495cda68..c04944dbf27a8ca7535d731d1912374571cb671f 100644
--- a/content/2.defense-systems/gao_her.md
+++ b/content/2.defense-systems/gao_her.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Her
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Her
 ## Example of genomic structure
 
 The Gao_Her system have been describe in a total of 2 subsystems.
diff --git a/content/2.defense-systems/gao_hhe.md b/content/2.defense-systems/gao_hhe.md
index 5773083c043814f7eeeb440ee89f2fe883b55790..ec48ec7c6a55e5f8144ed8c30751bd647f701d9f 100644
--- a/content/2.defense-systems/gao_hhe.md
+++ b/content/2.defense-systems/gao_hhe.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Hhe
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Hhe
 ## Example of genomic structure
 
 The Gao_Hhe system is composed of one protein: HheA.
diff --git a/content/2.defense-systems/gao_iet.md b/content/2.defense-systems/gao_iet.md
index 2fc12bc039c235895154536cc3f5132a7b929abb..96063cef40feb46e395fc88ef22248d245c411f7 100644
--- a/content/2.defense-systems/gao_iet.md
+++ b/content/2.defense-systems/gao_iet.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Iet
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Iet
 ## Example of genomic structure
 
 The Gao_Iet system is composed of 2 proteins: IetS and, IetA.
diff --git a/content/2.defense-systems/gao_mza.md b/content/2.defense-systems/gao_mza.md
index 0bcc8a4b5ee9c89b27d7a8e3b9d6ad2fa2e25993..c2e022124f2f7cc6dec09bccca6c2eac1e8bc94b 100644
--- a/content/2.defense-systems/gao_mza.md
+++ b/content/2.defense-systems/gao_mza.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Mza
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Mza
 ## Example of genomic structure
 
 The Gao_Mza system is composed of 5 proteins: MzaB, MzaC, MzaA, MzaD and, MzaE.
diff --git a/content/2.defense-systems/gao_ppl.md b/content/2.defense-systems/gao_ppl.md
index a07510399d023930eb6376a27b17b86cc4a83540..c6146a4bc0d62da845b6fc855208fa950fd79cbb 100644
--- a/content/2.defense-systems/gao_ppl.md
+++ b/content/2.defense-systems/gao_ppl.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Ppl
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Ppl
 ## Example of genomic structure
 
 The Gao_Ppl system is composed of one protein: PplA.
diff --git a/content/2.defense-systems/gao_qat.md b/content/2.defense-systems/gao_qat.md
index e9633099d1ce111f27dd6bc71a80712f61648a34..a0ac3c7d13b1e51f730b9e603720bb833d75dc87 100644
--- a/content/2.defense-systems/gao_qat.md
+++ b/content/2.defense-systems/gao_qat.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Qat
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Qat
 ## Example of genomic structure
 
 The Gao_Qat system is composed of 4 proteins: QatA, QatB, QatC and, QatD.
diff --git a/content/2.defense-systems/gao_rl.md b/content/2.defense-systems/gao_rl.md
index 92ba172f661179195f1dbbbbd6665449c88d4da5..472ca62222bfb748b58a248d718cdd7af285ab33 100644
--- a/content/2.defense-systems/gao_rl.md
+++ b/content/2.defense-systems/gao_rl.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_RL
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_RL
 ## Example of genomic structure
 
 The Gao_RL system is composed of 4 proteins: RL_D, RL_C, RL_B and, RL_A.
diff --git a/content/2.defense-systems/gao_tery.md b/content/2.defense-systems/gao_tery.md
index aea8b0c378a954e12227bfb8301512d95ec0f088..735ea6c22cf18b8c016a28fca186253b3ff5f04d 100644
--- a/content/2.defense-systems/gao_tery.md
+++ b/content/2.defense-systems/gao_tery.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_TerY
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_TerY
 ## Example of genomic structure
 
 The Gao_TerY system is composed of 3 proteins: TerYC, TerYB and, TerYA.
diff --git a/content/2.defense-systems/gao_tmn.md b/content/2.defense-systems/gao_tmn.md
index e0fe7c80c990f2dbc0592c14aaec7ce020fa0101..d92f39d2e414a0daef68f56995b09fc2f0d7899d 100644
--- a/content/2.defense-systems/gao_tmn.md
+++ b/content/2.defense-systems/gao_tmn.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Tmn
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Tmn
 ## Example of genomic structure
 
 The Gao_Tmn system is composed of one protein: TmnA.
diff --git a/content/2.defense-systems/gao_upx.md b/content/2.defense-systems/gao_upx.md
index ab9645b3cfb6378b634b28a85820544bbb5fc2da..d2def5a246cf6eef26243e31c179cf6b28ce0da6 100644
--- a/content/2.defense-systems/gao_upx.md
+++ b/content/2.defense-systems/gao_upx.md
@@ -1,7 +1,16 @@
 ---
 title: Gao_Upx
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Gao_Upx
 ## Example of genomic structure
 
 The Gao_Upx system is composed of one protein: UpxA.
diff --git a/content/2.defense-systems/gasdermin.md b/content/2.defense-systems/gasdermin.md
index 38046e6409c3d0391786b784524d29850e4041ba..c69a028a4a9e02c4f5bb031f5b499447767ae151 100644
--- a/content/2.defense-systems/gasdermin.md
+++ b/content/2.defense-systems/gasdermin.md
@@ -1,7 +1,16 @@
 ---
 title: GasderMIN
+tableColumns:
+    article:
+      doi: 10.1126/science.abj8432
+      abstract: |
+Gasdermin proteins form large membrane pores in human cells that release immune cytokines and induce lytic cell death. Gasdermin pore formation is triggered by caspase-mediated cleavage during inflammasome signaling and is critical for defense against pathogens and cancer. We discovered gasdermin homologs encoded in bacteria that defended against phages and executed cell death. Structures of bacterial gasdermins revealed a conserved pore-forming domain that was stabilized in the inactive state with a buried lipid modification. Bacterial gasdermins were activated by dedicated caspase-like proteases that catalyzed site-specific cleavage and the removal of an inhibitory C-terminal peptide. Release of autoinhibition induced the assembly of large and heterogeneous pores that disrupted membrane integrity. Thus, pyroptosis is an ancient form of regulated cell death shared between bacteria and animals.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Membrane disrupting
 ---
 
+# GasderMIN
 ## Example of genomic structure
 
 The GasderMIN system is composed of one protein: bGSDM.
diff --git a/content/2.defense-systems/gp29_gp30.md b/content/2.defense-systems/gp29_gp30.md
index f75f51a2d09ee06b520a00f1b1518b5c1fa6c81c..8a4ce6ca6036d76a71899a1b076eb0807f07b6b3 100644
--- a/content/2.defense-systems/gp29_gp30.md
+++ b/content/2.defense-systems/gp29_gp30.md
@@ -1,7 +1,13 @@
 ---
 title: gp29_gp30
+tableColumns:
+    article:
+      doi: 10.1038/nmicrobiol.2016.251
+      abstract: |
+Temperate phages are common, and prophages are abundant residents of sequenced bacterial genomes. Mycobacteriophages are viruses that infect mycobacterial hosts including Mycobacterium tuberculosis and Mycobacterium smegmatis, encompass substantial genetic diversity and are commonly temperate. Characterization of ten Cluster N temperate mycobacteriophages revealed at least five distinct prophage-expressed viral defence systems that interfere with the infection of lytic and temperate phages that are either closely related (homotypic defence) or unrelated (heterotypic defence) to the prophage. Target specificity is unpredictable, ranging from a single target phage to one-third of those tested. The defence systems include a single-subunit restriction system, a heterotypic exclusion system and a predicted (p)ppGpp synthetase, which blocks lytic phage growth, promotes bacterial survival and enables efficient lysogeny. The predicted (p)ppGpp synthetase coded by the Phrann prophage defends against phage Tweety infection, but Tweety codes for a tetrapeptide repeat protein, gp54, which acts as a highly effective counter-defence system. Prophage-mediated viral defence offers an efficient mechanism for bacterial success in host–virus dynamics, and counter-defence promotes phage co-evolution.
 ---
 
+# gp29_gp30
 ## Example of genomic structure
 
 The gp29_gp30 system is composed of 2 proteins: gp30 and, gp29.
diff --git a/content/2.defense-systems/hachiman.md b/content/2.defense-systems/hachiman.md
index 79867502662882a52dca777d951e7f47ce795993..916c4ead929cc6ba727e122dd833645ed0a7f5a3 100644
--- a/content/2.defense-systems/hachiman.md
+++ b/content/2.defense-systems/hachiman.md
@@ -1,7 +1,16 @@
 ---
 title: Hachiman
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Hachiman
 ## Description
 
 Hachiman Type 1 systems were the first discovered and can be found in 3.4% of microbial genomes (1). Hachiman Type 1 systems are encoded by two genes, *hamA* (annotated as a Domain of Unknown Function, DUF) and *hamB* (annotated as a helicase) (1). 
diff --git a/content/2.defense-systems/isg15-like.md b/content/2.defense-systems/isg15-like.md
index 7d4789da4694e74b9188d8c7cde43c9c2abdf619..02905798e7c5d563c0a63a689afd2a7521100c56 100644
--- a/content/2.defense-systems/isg15-like.md
+++ b/content/2.defense-systems/isg15-like.md
@@ -1,7 +1,16 @@
 ---
 title: ISG15-like
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# ISG15-like
 ## Example of genomic structure
 
 The ISG15-like system is composed of 4 proteins: BilD, BilC, BilB and, BilA.
diff --git a/content/2.defense-systems/kiwa.md b/content/2.defense-systems/kiwa.md
index 6f77579d4625c2d89f4e9c8d284d1086683b4b17..7958eb5d25f21160bec44873b51a4da300ce5060 100644
--- a/content/2.defense-systems/kiwa.md
+++ b/content/2.defense-systems/kiwa.md
@@ -1,7 +1,16 @@
 ---
 title: Kiwa
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Kiwa
 ## Example of genomic structure
 
 The Kiwa system is composed of 2 proteins: KwaA and, KwaB.
diff --git a/content/2.defense-systems/lamassu-fam.md b/content/2.defense-systems/lamassu-fam.md
index c7ef58acfd09268ad1e4e46b42dded866dd7c3d3..401c2dca41672c96dd4d6ee22c2d2e12006d512b 100644
--- a/content/2.defense-systems/lamassu-fam.md
+++ b/content/2.defense-systems/lamassu-fam.md
@@ -1,7 +1,16 @@
 ---
 title: Lamassu-Fam
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Diverse (Nucleic acid degrading (?), Nucleotide modifying (?), Membrane disrupting (?))
 ---
 
+# Lamassu-Fam
 ## Description
 
 The original types of Lamassu systems are Lamassu Type 1 and 2. They both necessarily comprise two genes *lmuA* and *lmuB*, to which a third gene (*lmuC*) is added in the case of Lamassu Type 2.  
diff --git a/content/2.defense-systems/lit.md b/content/2.defense-systems/lit.md
index d103914badf5f106ac90551552081fc459799ade..1e9c0bdc71d73645f4d5c4ecfbdfbddd77965f1f 100644
--- a/content/2.defense-systems/lit.md
+++ b/content/2.defense-systems/lit.md
@@ -1,7 +1,16 @@
 ---
 title: Lit
+tableColumns:
+    article:
+      doi: 10.1186/1743-422X-7-360
+      abstract: |
+Over 50 years of biological research with bacteriophage T4 includes notable discoveries in post-transcriptional control, including the genetic code, mRNA, and tRNA; the very foundations of molecular biology. In this review we compile the past 10 - 15 year literature on RNA-protein interactions with T4 and some of its related phages, with particular focus on advances in mRNA decay and processing, and on translational repression. Binding of T4 proteins RegB, RegA, gp32 and gp43 to their cognate target RNAs has been characterized. For several of these, further study is needed for an atomic-level perspective, where resolved structures of RNA-protein complexes are awaiting investigation. Other features of post-transcriptional control are also summarized. These include: RNA structure at translation initiation regions that either inhibit or promote translation initiation; programmed translational bypassing, where T4 orchestrates ribosome bypass of a 50 nucleotide mRNA sequence; phage exclusion systems that involve T4-mediated activation of a latent endoribonuclease (PrrC) and cofactor-assisted activation of EF-Tu proteolysis (Gol-Lit); and potentially important findings on ADP-ribosylation (by Alt and Mod enzymes) of ribosome-associated proteins that might broadly impact protein synthesis in the infected cell. Many of these problems can continue to be addressed with T4, whereas the growing database of T4-related phage genome sequences provides new resources and potentially new phage-host systems to extend the work into a broader biological, evolutionary context.
+    Sensor: Monitoring host integrity
+    Activator: Direct
+    Effector: Other (Cleaves an elongation factor, inhibiting cellular translation
 ---
 
+# Lit
 ## Example of genomic structure
 
 The Lit system is composed of one protein: Lit.
diff --git a/content/2.defense-systems/menshen.md b/content/2.defense-systems/menshen.md
index e904100100d105ca035b74ca3a023c31fcab87dc..4a6b779961adbb8b2a13a3ed788b2fc6a61035ac 100644
--- a/content/2.defense-systems/menshen.md
+++ b/content/2.defense-systems/menshen.md
@@ -1,7 +1,16 @@
 ---
 title: Menshen
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Menshen
 ## Example of genomic structure
 
 The Menshen system is composed of 3 proteins: NsnA, NsnB and, NsnC_2623244837.
diff --git a/content/2.defense-systems/mok_hok_sok.md b/content/2.defense-systems/mok_hok_sok.md
index b87ea0cb4e17db8fdb0afc884dd6027012d06a6a..046cd1e44bb12a625d4d7040fb329a8c307cca2a 100644
--- a/content/2.defense-systems/mok_hok_sok.md
+++ b/content/2.defense-systems/mok_hok_sok.md
@@ -1,7 +1,16 @@
 ---
 title: Mok_Hok_Sok
+tableColumns:
+    article:
+      doi: 10.1128/jb.178.7.2044-2050.1996
+      abstract: |
+The hok (host killing) and sok (suppressor of killing) genes (hok/sok) efficiently maintain the low-copy-number plasmid R1. To investigate whether the hok/sok locus evolved as a phage-exclusion mechanism, Escherichia coli cells that contain hok/sok on ...
+    Sensor: Monitoring of the host cell machinery (?)
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Mok_Hok_Sok
 ## Example of genomic structure
 
 The Mok_Hok_Sok system is composed of 2 proteins: Mok and, Hok.
diff --git a/content/2.defense-systems/mokosh.md b/content/2.defense-systems/mokosh.md
index 7fc1a69cdc4c3072a9b03e05d5b172b6cadf20ab..36555ab2c0f315cf08b5c268aa3b062209a9a687 100644
--- a/content/2.defense-systems/mokosh.md
+++ b/content/2.defense-systems/mokosh.md
@@ -1,7 +1,16 @@
 ---
 title: Mokosh
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Mokosh
 ## Example of genomic structure
 
 The Mokosh system have been describe in a total of 2 subsystems.
diff --git a/content/2.defense-systems/mqsrac.md b/content/2.defense-systems/mqsrac.md
index 18e3160297417ac5123cbdb65825924b9be3c02e..671ba38e5d9e6a59aec5b94a9bbc0f9b87cda269 100644
--- a/content/2.defense-systems/mqsrac.md
+++ b/content/2.defense-systems/mqsrac.md
@@ -1,7 +1,13 @@
 ---
 title: MqsRAC
+tableColumns:
+    article:
+      doi: 10.1101/2023.02.25.529695
+      abstract: |
+Myriad bacterial anti-phage systems have been described and often the mechanism of programmed cell death is invoked for phage inhibition. However, there is little evidence of ‘suicide’ under physiological conditions for these systems. Instead of death to stop phage propagation, we show here that persister cells, i.e., transiently-tolerant, dormant, antibiotic-insensitive cells, are formed and survive using the Escherichia coli C496_10 tripartite toxin/antitoxin system MqsR/MqsA/MqsC to inhibit T2 phage. Specifically, MqsR/MqsA/MqsC inhibited T2 phage by one million-fold and reduced T2 titers by 500-fold. During T2 phage attack, in the presence of MqsR/MqsA/MqsC, evidence of persistence include the single-cell physiological change of reduced metabolism (via flow cytometry), increased spherical morphology (via transmission electron microscopy), and heterogeneous resuscitation. Critically, we found restriction-modification systems (primarily EcoK McrBC) work in concert with the toxin/antitoxin system to inactivate phage, likely while the cells are in the persister state. Phage attack also induces persistence in Klebsiella and Pseudomonas spp. Hence, phage attack invokes a stress response similar to antibiotics, starvation, and oxidation, which leads to persistence, and this dormant state likely allows restriction/modification systems to clear phage DNA.
 ---
 
+# MqsRAC
 ## Example of genomic structure
 
 The MqsRAC system is composed of 2 proteins: mqsR and, mqsC.
diff --git a/content/2.defense-systems/nhi.md b/content/2.defense-systems/nhi.md
index 884324a8d5e1f32e10b2602980bb6d396021458d..a99c1293e17010e096ef21e422b7738c8c8e6db3 100644
--- a/content/2.defense-systems/nhi.md
+++ b/content/2.defense-systems/nhi.md
@@ -1,7 +1,16 @@
 ---
 title: Nhi
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.03.001
+      abstract: |
+The perpetual arms race between bacteria and their viruses (phages) has given rise to diverse immune systems, including restriction-modification and CRISPR-Cas, which sense and degrade phage-derived nucleic acids. These complex systems rely upon production and maintenance of multiple components to achieve antiphage defense. However, the prevalence and effectiveness of minimal, single-component systems that cleave DNA remain unknown. Here, we describe a unique mode of nucleic acid immunity mediated by a single enzyme with nuclease and helicase activities, herein referred to as Nhi (nuclease-helicase immunity). This enzyme provides robust protection against diverse staphylococcal phages and prevents phage DNA accumulation in cells stripped of all other known defenses. Our observations support a model in which Nhi targets and degrades phage-specific replication intermediates. Importantly, Nhi homologs are distributed in diverse bacteria and exhibit functional conservation, highlighting the versatility of such compact weapons as major players in antiphage defense.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Nucleic acid degrading (?)
 ---
 
+# Nhi
 ## Example of genomic structure
 
 The Nhi system is composed of one protein: Nhi.
diff --git a/content/2.defense-systems/nixi.md b/content/2.defense-systems/nixi.md
index a8b8e6db84d283d5c18c677635565e449c384735..7b3836f1e0ba8f39aef728f78fd075dd271daa9d 100644
--- a/content/2.defense-systems/nixi.md
+++ b/content/2.defense-systems/nixi.md
@@ -1,7 +1,16 @@
 ---
 title: NixI
+tableColumns:
+    article:
+      doi: 10.1101/2021.07.12.452122
+      abstract: |
+PLEs are phage parasites integrated into the chromosome of epidemic Vibrio cholerae. In response to infection by its viral host ICP1, PLE excises, replicates and hijacks ICP1 structural components for transduction. Through an unknown mechanism PLE prevents ICP1 from transitioning to rolling circle replication (RCR), a prerequisite for efficient packaging of the viral genome. Here, we characterize a PLE-encoded nuclease, NixI, that blocks phage development likely by nicking ICP1Â’s genome as it transitions to RCR. NixI-dependent cleavage sites appear in ICP1Â’s genome during infection of PLE(+) V. cholerae. Purified NixI demonstrates in vitro specificity for sites in ICP1Â’s genome and NixI activity is enhanced by a putative specificity determinant co-expressed with NixI during phage infection. Importantly, NixI is sufficient to limit ICP1 genome replication and eliminate progeny production. We identify distant NixI homologs in an expanded family of putative phage satellites in Vibrios that lack nucleotide homology to PLEs but nonetheless share genomic synteny with PLEs. More generally, our results reveal a previously unknown mechanism deployed by phage parasites to limit packaging of their viral hostsÂ’ genome and highlight the prominent role of nuclease effectors as weapons in the arms race between antagonizing genomes.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Nucleic acid degrading
 ---
 
+# NixI
 ## Example of genomic structure
 
 The NixI system is composed of 2 proteins: NixI and, Stix.
diff --git a/content/2.defense-systems/nlr.md b/content/2.defense-systems/nlr.md
index b3102c934bbe46c6cb1749d6fe7bb413fdd9057b..e32466e1c0fe463940bb4bd5bef1a460192707f9 100644
--- a/content/2.defense-systems/nlr.md
+++ b/content/2.defense-systems/nlr.md
@@ -1,7 +1,16 @@
 ---
 title: NLR
+tableColumns:
+    article:
+      doi: 10.1101/2022.07.19.500537
+      abstract: |
+Bacteria use a wide range of immune systems to counter phage infection. A subset of these genes share homology with components of eukaryotic immune systems, suggesting that eukaryotes horizontally acquired certain innate immune genes from bacteria. Here we show that proteins containing a NACHT module, the central feature of the animal nucleotide-binding domain and leucine-rich repeat containing gene family (NLRs), are found in bacteria and defend against phages. NACHT proteins are widespread in bacteria, provide immunity against both DNA and RNA phages, and display the characteristic C-terminal sensor, central NACHT, and N-terminal effector modules. Some bacterial NACHT proteins have domain architectures similar to human NLRs that are critical components of inflammasomes. Human disease-associated NLR mutations that cause stimulus-independent activation of the inflammasome also activate bacterial NACHT proteins, supporting a shared signaling mechanism. This work establishes that NACHT module-containing proteins are ancient mediators of innate immunity across the tree of life.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# NLR
 ## Example of genomic structure
 
 The NLR system have been describe in a total of 2 subsystems.
diff --git a/content/2.defense-systems/old_exonuclease.md b/content/2.defense-systems/old_exonuclease.md
index 9df6fa039d4254760871e8294b041090b04fdf5c..9e309a33bb8f80fffe76abba5a59afa04a700c3a 100644
--- a/content/2.defense-systems/old_exonuclease.md
+++ b/content/2.defense-systems/old_exonuclease.md
@@ -1,7 +1,16 @@
 ---
 title: Old_exonuclease
+tableColumns:
+    article:
+      doi: 10.1128/jb.177.3.497-501.1995
+      abstract: |
+The Old protein of bacteriophage P2 is responsible for interference with the growth of phage lambda and for killing of recBC mutant Escherichia coli. We have purified Old fused to the maltose-binding protein to 95% purity and characterized its enzymatic properties. The Old protein fused to maltose-binding protein has exonuclease activity on double-stranded DNA as well as nuclease activity on single-stranded DNA and RNA. The direction of digestion of double-stranded DNA is from 5' to 3', and digestion initiates at either the 5'-phosphoryl or 5'-hydroxyl terminus. The nuclease is active on nicked circular DNA, degrades DNA in a processive manner, and releases 5'-phosphoryl mononucleotides.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Old_exonuclease
 ## Example of genomic structure
 
 The Old_exonuclease system is composed of one protein: Old_exonuclease.
diff --git a/content/2.defense-systems/olokun.md b/content/2.defense-systems/olokun.md
index 4a8cd69a6ed6f975fb557c6cb34ffdf4d3ddaecc..400b9b6da8ddac5ec1955da6fdb3eb1d38f96121 100644
--- a/content/2.defense-systems/olokun.md
+++ b/content/2.defense-systems/olokun.md
@@ -1,7 +1,16 @@
 ---
 title: Olokun
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Olokun
 ## Example of genomic structure
 
 The Olokun system is composed of 2 proteins: OloA and, OloB.
diff --git a/content/2.defense-systems/pago.md b/content/2.defense-systems/pago.md
index fde9b1235730add14413de5f760004683e7784ff..230037909c7ac09da33d2343345ea1509dbc16ae 100644
--- a/content/2.defense-systems/pago.md
+++ b/content/2.defense-systems/pago.md
@@ -1,7 +1,17 @@
 ---
 title: pAgo
+tableColumns:
+    article:
+      doi: 10.1186/1745-6150-4-29
+      abstract: |
+BACKGROUND: In eukaryotes, RNA interference (RNAi) is a major mechanism of defense against viruses and transposable elements as well of regulating translation of endogenous mRNAs. The RNAi systems recognize the target RNA molecules via small guide RNAs that are completely or partially complementary to a region of the target. Key components of the RNAi systems are proteins of the Argonaute-PIWI family some of which function as slicers, the nucleases that cleave the target RNA that is base-paired to a guide RNA. Numerous prokaryotes possess the CRISPR-associated system (CASS) of defense against phages and plasmids that is, in part, mechanistically analogous but not homologous to eukaryotic RNAi systems. Many prokaryotes also encode homologs of Argonaute-PIWI proteins but their functions remain unknown. RESULTS: We present a detailed analysis of Argonaute-PIWI protein sequences and the genomic neighborhoods of the respective genes in prokaryotes. Whereas eukaryotic Ago/PIWI proteins always contain PAZ (oligonucleotide binding) and PIWI (active or inactivated nuclease) domains, the prokaryotic Argonaute homologs (pAgos) fall into two major groups in which the PAZ domain is either present or absent. The monophyly of each group is supported by a phylogenetic analysis of the conserved PIWI-domains. Almost all pAgos that lack a PAZ domain appear to be inactivated, and the respective genes are associated with a variety of predicted nucleases in putative operons. An additional, uncharacterized domain that is fused to various nucleases appears to be a unique signature of operons encoding the short (lacking PAZ) pAgo form. By contrast, almost all PAZ-domain containing pAgos are predicted to be active nucleases. Some proteins of this group (e.g., that from Aquifex aeolicus) have been experimentally shown to possess nuclease activity, and are not typically associated with genes for other (putative) nucleases. Given these observations, the apparent extensive horizontal transfer of pAgo genes, and their common, statistically significant over-representation in genomic neighborhoods enriched in genes encoding proteins involved in the defense against phages and/or plasmids, we hypothesize that pAgos are key components of a novel class of defense systems. The PAZ-domain containing pAgos are predicted to directly destroy virus or plasmid nucleic acids via their nuclease activity, whereas the apparently inactivated, PAZ-lacking pAgos could be structural subunits of protein complexes that contain, as active moieties, the putative nucleases that we predict to be co-expressed with these pAgos. All these nucleases are predicted to be DNA endonucleases, so it seems most probable that the putative novel phage/plasmid-defense system targets phage DNA rather than mRNAs. Given that in eukaryotic RNAi systems, the PAZ domain binds a guide RNA and positions it on the complementary region of the target, we further speculate that pAgos function on a similar principle (the guide being either DNA or RNA), and that the uncharacterized domain found in putative operons with the short forms of pAgos is a functional substitute for the PAZ domain. CONCLUSION: The hypothesis that pAgos are key components of a novel prokaryotic immune system that employs guide RNA or DNA molecules to degrade nucleic acids of invading mobile elements implies a functional analogy with the prokaryotic CASS and a direct evolutionary connection with eukaryotic RNAi. The predictions of the hypothesis including both the activities of pAgos and those of the associated endonucleases are readily amenable to experimental tests.
+    Sensor: Detecting invading nucleic acid
+    Activator: Direct
+    Effector: Diverse (Nucleotide modifying 
+Membrane disrupting)
 ---
 
+# pAgo
 ## Example of genomic structure
 
 The pAgo system is composed of one protein: pAgo_Short.
diff --git a/content/2.defense-systems/pd-lambda-1.md b/content/2.defense-systems/pd-lambda-1.md
index db4f0937c932fd81e32a6bbd5c52f0be45f364b2..3d350d8df4912b1bfddf7361df7d5ddcbfb0f658 100644
--- a/content/2.defense-systems/pd-lambda-1.md
+++ b/content/2.defense-systems/pd-lambda-1.md
@@ -1,7 +1,16 @@
 ---
 title: PD-Lambda-1
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-Lambda-1
 ## Example of genomic structure
 
 The PD-Lambda-1 system is composed of one protein: PD-Lambda-1.
diff --git a/content/2.defense-systems/pd-lambda-2.md b/content/2.defense-systems/pd-lambda-2.md
index a8316a74affbf71a0bdc44c52f663220542c5eb6..6a235edc0e3414872e2b5c9dbf21a348ccd7913d 100644
--- a/content/2.defense-systems/pd-lambda-2.md
+++ b/content/2.defense-systems/pd-lambda-2.md
@@ -1,7 +1,16 @@
 ---
 title: PD-Lambda-2
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-Lambda-2
 ## Example of genomic structure
 
 The PD-Lambda-2 system is composed of 3 proteins: PD-Lambda-2_C, PD-Lambda-2_B and, PD-Lambda-2_A.
diff --git a/content/2.defense-systems/pd-lambda-3.md b/content/2.defense-systems/pd-lambda-3.md
index 191f15c6eb29778440cbe31ca8a8c25e3beb2a4c..dacd6f40b6ed876140c01b0ec3cb4f9c967f12ce 100644
--- a/content/2.defense-systems/pd-lambda-3.md
+++ b/content/2.defense-systems/pd-lambda-3.md
@@ -1,7 +1,16 @@
 ---
 title: PD-Lambda-3
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-Lambda-3
 ## Example of genomic structure
 
 The PD-Lambda-3 system is composed of 2 proteins: PD-Lambda-3_B and, PD-Lambda-3_A.
diff --git a/content/2.defense-systems/pd-lambda-4.md b/content/2.defense-systems/pd-lambda-4.md
index c05e95f7d1774e4c9eed1fe82e51df1222679020..a22ee34334808fa4b4c8fe0741fb39beb9fdc643 100644
--- a/content/2.defense-systems/pd-lambda-4.md
+++ b/content/2.defense-systems/pd-lambda-4.md
@@ -1,7 +1,16 @@
 ---
 title: PD-Lambda-4
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-Lambda-4
 ## Example of genomic structure
 
 The PD-Lambda-4 system is composed of 2 proteins: PD-Lambda-4_A and, PD-Lambda-4_B.
diff --git a/content/2.defense-systems/pd-lambda-5.md b/content/2.defense-systems/pd-lambda-5.md
index 949f461b0190b0be52bd08551844f9f7bfc4fc86..b2b785e5e0b611ab9ddc6335107016cd46aee34b 100644
--- a/content/2.defense-systems/pd-lambda-5.md
+++ b/content/2.defense-systems/pd-lambda-5.md
@@ -1,7 +1,16 @@
 ---
 title: PD-Lambda-5
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-Lambda-5
 ## Example of genomic structure
 
 The PD-Lambda-5 system is composed of 2 proteins: PD-Lambda-5_A and, PD-Lambda-5_B.
diff --git a/content/2.defense-systems/pd-lambda-6.md b/content/2.defense-systems/pd-lambda-6.md
index 1c4c22720b7c938b61ea7f06ad06fbc5357aef4e..abb03287f1c7e2588d06a335658984a504c5e633 100644
--- a/content/2.defense-systems/pd-lambda-6.md
+++ b/content/2.defense-systems/pd-lambda-6.md
@@ -1,7 +1,16 @@
 ---
 title: PD-Lambda-6
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-Lambda-6
 ## Example of genomic structure
 
 The PD-Lambda-6 system is composed of one protein: PD-Lambda-6.
diff --git a/content/2.defense-systems/pd-t4-1.md b/content/2.defense-systems/pd-t4-1.md
index bf38ceee698240b2eb4eb222a088b658ef0c8a2b..d7d3c615bf5a5a75a00c44613d2c64b99f15751a 100644
--- a/content/2.defense-systems/pd-t4-1.md
+++ b/content/2.defense-systems/pd-t4-1.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-1
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-1
 ## Example of genomic structure
 
 The PD-T4-1 system is composed of one protein: PD-T4-1.
diff --git a/content/2.defense-systems/pd-t4-10.md b/content/2.defense-systems/pd-t4-10.md
index cf7a258f070f404242e906ef4cedd55592f32eea..bea4b40a8f5646a635943fa895d6c4a013ebe723 100644
--- a/content/2.defense-systems/pd-t4-10.md
+++ b/content/2.defense-systems/pd-t4-10.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-10
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-10
 ## Example of genomic structure
 
 The PD-T4-10 system is composed of 2 proteins: PD-T4-10_B and, PD-T4-10_A.
diff --git a/content/2.defense-systems/pd-t4-2.md b/content/2.defense-systems/pd-t4-2.md
index 8a17374ec5a181b7408b5ba62ee9f1caeaed095c..6a386de220afdba07f9b57533198ded41d93b501 100644
--- a/content/2.defense-systems/pd-t4-2.md
+++ b/content/2.defense-systems/pd-t4-2.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-2
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-2
 ## Example of genomic structure
 
 The PD-T4-2 system is composed of 2 proteins: PD-T4-2_B and, PD-T4-2_A.
diff --git a/content/2.defense-systems/pd-t4-3.md b/content/2.defense-systems/pd-t4-3.md
index 9339d524a3cee996fa927647927ccb57f43e048f..36084e33e4171a2a79a111e0ec520ec5f6fea230 100644
--- a/content/2.defense-systems/pd-t4-3.md
+++ b/content/2.defense-systems/pd-t4-3.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-3
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-3
 ## Example of genomic structure
 
 The PD-T4-3 system is composed of one protein: PD-T4-3.
diff --git a/content/2.defense-systems/pd-t4-4.md b/content/2.defense-systems/pd-t4-4.md
index bb8ccc813a0b1bca32f416592cabcf4f5abc291f..6763ffd43e2664e1ce569adb0495d60ee9deb48c 100644
--- a/content/2.defense-systems/pd-t4-4.md
+++ b/content/2.defense-systems/pd-t4-4.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-4
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-4
 ## Example of genomic structure
 
 The PD-T4-4 system is composed of 2 proteins: PD-T4-4_A and, PD-T4-4_B.
diff --git a/content/2.defense-systems/pd-t4-5.md b/content/2.defense-systems/pd-t4-5.md
index 99a129137e05c6c0f137bc59e2d0e119519d2699..c51a01deb58b646d00da0eac30e052247cf70300 100644
--- a/content/2.defense-systems/pd-t4-5.md
+++ b/content/2.defense-systems/pd-t4-5.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-5
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-5
 ## Example of genomic structure
 
 The PD-T4-5 system is composed of one protein: PD-T4-5.
diff --git a/content/2.defense-systems/pd-t4-6.md b/content/2.defense-systems/pd-t4-6.md
index 5091f597c4950f461eace8dfdd3e164d8e5054e4..16283385f9fb36d81156448a69f77120128bc187 100644
--- a/content/2.defense-systems/pd-t4-6.md
+++ b/content/2.defense-systems/pd-t4-6.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-6
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-6
 ## Example of genomic structure
 
 The PD-T4-6 system is composed of one protein: PD-T4-6.
diff --git a/content/2.defense-systems/pd-t4-7.md b/content/2.defense-systems/pd-t4-7.md
index 93829d7878bab118365ae1b17419d3d3393ba2c6..18b58c183edeaa02be5aea797669b51a2fca1aeb 100644
--- a/content/2.defense-systems/pd-t4-7.md
+++ b/content/2.defense-systems/pd-t4-7.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-7
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-7
 ## Example of genomic structure
 
 The PD-T4-7 system is composed of one protein: PD-T4-7.
diff --git a/content/2.defense-systems/pd-t4-8.md b/content/2.defense-systems/pd-t4-8.md
index 6fbc3400ab12c5cdb514727cacbb62fbfc22cd72..4fd5327ff636f5d4c08725f54c297fcb0c349c0e 100644
--- a/content/2.defense-systems/pd-t4-8.md
+++ b/content/2.defense-systems/pd-t4-8.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-8
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-8
 ## Example of genomic structure
 
 The PD-T4-8 system is composed of one protein: PD-T4-8.
diff --git a/content/2.defense-systems/pd-t4-9.md b/content/2.defense-systems/pd-t4-9.md
index fe9b8f669480c1b28790ad73d279288b193f239c..a8b4dd159c999a6c429edb7cac64a5361c7f113c 100644
--- a/content/2.defense-systems/pd-t4-9.md
+++ b/content/2.defense-systems/pd-t4-9.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T4-9
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T4-9
 ## Example of genomic structure
 
 The PD-T4-9 system is composed of 3 proteins: PD-T4-9_C, PD-T4-9_B and, PD-T4-9_A.
diff --git a/content/2.defense-systems/pd-t7-1.md b/content/2.defense-systems/pd-t7-1.md
index cbb34acfadee4199b4962c96b6bf8e1becba80f3..271ada5784460f16a6248da9e5805a85ff3638a6 100644
--- a/content/2.defense-systems/pd-t7-1.md
+++ b/content/2.defense-systems/pd-t7-1.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T7-1
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T7-1
 ## Example of genomic structure
 
 The PD-T7-1 system is composed of one protein: PD-T7-1.
diff --git a/content/2.defense-systems/pd-t7-2.md b/content/2.defense-systems/pd-t7-2.md
index 4027829eec055cb668ee5b0116e6f4839591d03a..1e56bda4469ee0c1f066dc8a1c840429a4254774 100644
--- a/content/2.defense-systems/pd-t7-2.md
+++ b/content/2.defense-systems/pd-t7-2.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T7-2
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T7-2
 ## Example of genomic structure
 
 The PD-T7-2 system is composed of 2 proteins: PD-T7-2_A and, PD-T7-2_B.
diff --git a/content/2.defense-systems/pd-t7-3.md b/content/2.defense-systems/pd-t7-3.md
index 7ff84cc318fc6504f28e3fadfaf0925470d1113c..0f8aa0a4c2986a97ca9264f6b9cd0373c7515c33 100644
--- a/content/2.defense-systems/pd-t7-3.md
+++ b/content/2.defense-systems/pd-t7-3.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T7-3
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T7-3
 ## Example of genomic structure
 
 The PD-T7-3 system is composed of one protein: PD-T7-3.
diff --git a/content/2.defense-systems/pd-t7-4.md b/content/2.defense-systems/pd-t7-4.md
index d817d2d4fb04126721159a55315522129e0ac31f..6490f29facd55392e793c30e3d6f8cef086b5515 100644
--- a/content/2.defense-systems/pd-t7-4.md
+++ b/content/2.defense-systems/pd-t7-4.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T7-4
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T7-4
 ## Example of genomic structure
 
 The PD-T7-4 system is composed of one protein: PD-T7-4.
diff --git a/content/2.defense-systems/pd-t7-5.md b/content/2.defense-systems/pd-t7-5.md
index 28277c7ea86ee945d0df0f08f24625ca0d611956..2a6667bb914cf2376bc2f91d9d30f45b957615b1 100644
--- a/content/2.defense-systems/pd-t7-5.md
+++ b/content/2.defense-systems/pd-t7-5.md
@@ -1,7 +1,16 @@
 ---
 title: PD-T7-5
+tableColumns:
+    article:
+      doi: 10.1038/s41564-022-01219-4
+      abstract: |
+The ancient, ongoing coevolutionary battle between bacteria and their viruses, bacteriophages, has given rise to sophisticated immune systems including restriction-modification and CRISPR-Cas. Many additional anti-phage systems have been identified using computational approaches based on genomic co-location within defence islands, but these screens may not be exhaustive. Here we developed an experimental selection scheme agnostic to genomic context to identify defence systems in 71 diverse E. coli strains. Our results unveil 21 conserved defence systems, none of which were previously detected as enriched in defence islands. Additionally, our work indicates that intact prophages and mobile genetic elements are primary reservoirs and distributors of defence systems in E. coli, with defence systems typically carried in specific locations or hotspots. These hotspots encode dozens of additional uncharacterized defence system candidates. Our findings reveal an extended landscape of antiviral immunity in E. coli and provide an approach for mapping defence systems in other species.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PD-T7-5
 ## Example of genomic structure
 
 The PD-T7-5 system is composed of one protein: PD-T7-5.
diff --git a/content/2.defense-systems/pfiat.md b/content/2.defense-systems/pfiat.md
index f9911b0a60853dc9200fb33c97c9d3104feb554c..47655bc0e2e8b8223aa915892202565d870893c2 100644
--- a/content/2.defense-systems/pfiat.md
+++ b/content/2.defense-systems/pfiat.md
@@ -1,7 +1,16 @@
 ---
 title: PfiAT
+tableColumns:
+    article:
+      doi: 10.1111/1751-7915.13570
+      abstract: |
+Pf prophages are ssDNA filamentous prophages that are prevalent among various Pseudomonas aeruginosa strains. The genomes of Pf prophages contain not only core genes encoding functions involved in phage replication, structure and assembly but also accessory genes. By studying the accessory genes in the Pf4 prophage in P. aeruginosa PAO1, we provided experimental evidence to demonstrate that PA0729 and the upstream ORF Rorf0727 near the right attachment site of Pf4 form a type II toxin/antitoxin (TA) pair. Importantly, we found that the deletion of the toxin gene PA0729 greatly increased Pf4 phage production. We thus suggest the toxin PA0729 be named PfiT for Pf4 inhibition toxin and Rorf0727 be named PfiA for PfiT antitoxin. The PfiT toxin directly binds to PfiA and functions as a corepressor of PfiA for the TA operon. The PfiAT complex exhibited autoregulation by binding to a palindrome (5'-AATTCN5 GTTAA-3') overlapping the -35 region of the TA operon. The deletion of pfiT disrupted TA autoregulation and activated pfiA expression. Additionally, the deletion of pfiT also activated the expression of the replication initiation factor gene PA0727. Moreover, the Pf4 phage released from the pfiT deletion mutant overcame the immunity provided by the phage repressor Pf4r. Therefore, this study reveals that the TA systems in Pf prophages can regulate phage production and phage immunity, providing new insights into the function of TAs in mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PfiAT
 ## Example of genomic structure
 
 The PfiAT system is composed of 2 proteins: PfiA and, PfiT.
diff --git a/content/2.defense-systems/pif.md b/content/2.defense-systems/pif.md
index ac07e1a2f9432816c7eb4cc936f6d2a302005050..45593ebb850f81abdbeaaed6fcb6a0074d5f1bb4 100644
--- a/content/2.defense-systems/pif.md
+++ b/content/2.defense-systems/pif.md
@@ -1,7 +1,16 @@
 ---
 title: Pif
+tableColumns:
+    article:
+      doi: 10.1007/BF00327934
+      abstract: |
+We report the molecular cloning of the pif region of the F plasmid and its physical dissection by subcloning and deletion analysis. Examination of the polypeptide products synthesized in maxicells by plasmids carrying defined pif sequences has shown that the region specifies at least two proteins of molecular weights 80,000 and 40,000, the genes for which appear to lie in the same transcriptional unit. In addition, analysis of pif-lacZ fusion plasmids has detected a pif promoter and determined the direction of transcription across the pif region.
+    Sensor: Sensing of phage protein
+    Activator: Unknown
+    Effector: Membrane disrupting (?)
 ---
 
+# Pif
 ## Example of genomic structure
 
 The Pif system is composed of 2 proteins: PifC and, PifA.
diff --git a/content/2.defense-systems/prrc.md b/content/2.defense-systems/prrc.md
index a83866c3eb013ddbf722e98effeb7d9e0d276e16..2f0986b6f1bb957812754c15910ea2ccc160078d 100644
--- a/content/2.defense-systems/prrc.md
+++ b/content/2.defense-systems/prrc.md
@@ -1,7 +1,16 @@
 ---
 title: PrrC
+tableColumns:
+    article:
+      doi: 10.1186/1743-422X-7-360
+      abstract: |
+Over 50 years of biological research with bacteriophage T4 includes notable discoveries in post-transcriptional control, including the genetic code, mRNA, and tRNA; the very foundations of molecular biology. In this review we compile the past 10 - 15 year literature on RNA-protein interactions with T4 and some of its related phages, with particular focus on advances in mRNA decay and processing, and on translational repression. Binding of T4 proteins RegB, RegA, gp32 and gp43 to their cognate target RNAs has been characterized. For several of these, further study is needed for an atomic-level perspective, where resolved structures of RNA-protein complexes are awaiting investigation. Other features of post-transcriptional control are also summarized. These include: RNA structure at translation initiation regions that either inhibit or promote translation initiation; programmed translational bypassing, where T4 orchestrates ribosome bypass of a 50 nucleotide mRNA sequence; phage exclusion systems that involve T4-mediated activation of a latent endoribonuclease (PrrC) and cofactor-assisted activation of EF-Tu proteolysis (Gol-Lit); and potentially important findings on ADP-ribosylation (by Alt and Mod enzymes) of ribosome-associated proteins that might broadly impact protein synthesis in the infected cell. Many of these problems can continue to be addressed with T4, whereas the growing database of T4-related phage genome sequences provides new resources and potentially new phage-host systems to extend the work into a broader biological, evolutionary context.
+    Sensor: Monitor the integrity of the bacterial cell machinery
+    Activator: Direct
+    Effector: Nucleic acid degrading
 ---
 
+# PrrC
 ## Example of genomic structure
 
 The PrrC system is composed of 4 proteins: EcoprrI, Type_I_S, PrrC and, Type_I_REases.
diff --git a/content/2.defense-systems/psyrta.md b/content/2.defense-systems/psyrta.md
index e1d7ae9f10c29e6e4f2d88f7fcc653e0923a0fd7..73ad3ad5becb1f7dc7a37a831015a2aed64eeabe 100644
--- a/content/2.defense-systems/psyrta.md
+++ b/content/2.defense-systems/psyrta.md
@@ -1,7 +1,16 @@
 ---
 title: PsyrTA
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# PsyrTA
 ## Example of genomic structure
 
 The PsyrTA system is composed of 2 proteins: PsyrT and, PsyrA.
diff --git a/content/2.defense-systems/pycsar.md b/content/2.defense-systems/pycsar.md
index a8b5ef7a1044446a9ae147b760c8a5289d50f15c..9261f2da4c1560fbeb8dc66f94a27496333f64e1 100644
--- a/content/2.defense-systems/pycsar.md
+++ b/content/2.defense-systems/pycsar.md
@@ -1,7 +1,17 @@
 ---
 title: Pycsar
+tableColumns:
+    article:
+      doi: 10.1016/j.cell.2021.09.031
+      abstract: |
+The cyclic pyrimidines 3',5'-cyclic cytidine monophosphate (cCMP) and 3',5'-cyclic uridine monophosphate (cUMP) have been reported in multiple organisms and cell types. As opposed to the cyclic nucleotides 3',5'-cyclic adenosine monophosphate (cAMP) and 3',5'-cyclic guanosine monophosphate (cGMP), which are second messenger molecules with well-established regulatory roles across all domains of life, the biological role of cyclic pyrimidines has remained unclear. Here we report that cCMP and cUMP are second messengers functioning in bacterial immunity against viruses. We discovered a family of bacterial pyrimidine cyclase enzymes that specifically synthesize cCMP and cUMP following phage infection and demonstrate that these molecules activate immune effectors that execute an antiviral response. A crystal structure of a uridylate cyclase enzyme from this family explains the molecular mechanism of selectivity for pyrimidines as cyclization substrates. Defense systems encoding pyrimidine cyclases, denoted here Pycsar (pyrimidine cyclase system for antiphage resistance), are widespread in prokaryotes. Our results assign clear biological function to cCMP and cUMP as immunity signaling molecules in bacteria.
+    Sensor: Unknown
+    Activator: Signaling molecules
+    Effector: Membrane disrupting
+Nucleotides modifying
 ---
 
+# Pycsar
 ## Example of genomic structure
 
 The Pycsar system is composed of 2 proteins: AG_cyclase and, Effector_TIR.
diff --git a/content/2.defense-systems/radar.md b/content/2.defense-systems/radar.md
index aaf9a41d18ad6e4fff9f69d878f00f1ad4de4154..0a2a890bbe8dff91c1e6f0498f5e9287e7773d53 100644
--- a/content/2.defense-systems/radar.md
+++ b/content/2.defense-systems/radar.md
@@ -1,7 +1,16 @@
 ---
 title: RADAR
+tableColumns:
+    article:
+      doi: 10.1126/science.aba0372
+      abstract: |
+Bacteria and archaea are frequently attacked by viruses and other mobile genetic elements and rely on dedicated antiviral defense systems, such as restriction endonucleases and CRISPR, to survive. The enormous diversity of viruses suggests that more types of defense systems exist than are currently known. By systematic defense gene prediction and heterologous reconstitution, here we discover 29 widespread antiviral gene cassettes, collectively present in 32% of all sequenced bacterial and archaeal genomes, that mediate protection against specific bacteriophages. These systems incorporate enzymatic activities not previously implicated in antiviral defense, including RNA editing and retron satellite DNA synthesis. In addition, we computationally predict a diverse set of other putative defense genes that remain to be characterized. These results highlight an immense array of molecular functions that microbes use against viruses.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Nucleic acid degrading
 ---
 
+# RADAR
 ## Description
 
 RADAR is comprised of two genes, encoding respectively for an adenosine triphosphatase (RdrA) and  a divergent adenosine deaminase (RdrB) (1), which are in some cases associated with a small membrane protein (RdrC or D) (1). 
diff --git a/content/2.defense-systems/retron.md b/content/2.defense-systems/retron.md
index ac65d092447e95306672f9f1ff454509c531d46f..73b156fda62b6ce2b62e481bd82d430a7363657d 100644
--- a/content/2.defense-systems/retron.md
+++ b/content/2.defense-systems/retron.md
@@ -1,7 +1,16 @@
 ---
 title: Retron
+tableColumns:
+    article:
+      doi: 10.1093/nar/gkaa1149
+      abstract: |
+Bacterial retrons consist of a reverse transcriptase (RT) and a contiguous non-coding RNA (ncRNA) gene. One third of annotated retrons carry additional open reading frames (ORFs), the contribution and significance of which in retron biology remains to be determined. In this study we developed a computational pipeline for the systematic prediction of genes specifically associated with retron RTs based on a previously reported large dataset representative of the diversity of prokaryotic RTs. We found that retrons generally comprise a tripartite system composed of the ncRNA, the RT and an additional protein or RT-fused domain with diverse enzymatic functions. These retron systems are highly modular, and their components have coevolved to different extents. Based on the additional module, we classified retrons into 13 types, some of which include additional variants. Our findings provide a basis for future studies on the biological function of retrons and for expanding their biotechnological applications.
+    Sensor: Monitor the integrity of the bacterial cell machinery
+    Activator: Unknown
+    Effector: Diverse
 ---
 
+# Retron
 ## Description
 
 Retrons are genetic elements constituted of a non-coding RNA (ncRNA) associated with a reverse-transcriptase (RT). The RT reverse-transcribes part of the ncRNA to generate an RNA-DNA hybrid molecule. Although the existence of retrons have been known for decades, their biological functions were unknown. Recent studies revealed that most retrons could in fact be anti-phage systems (1,2). 
diff --git a/content/2.defense-systems/rexab.md b/content/2.defense-systems/rexab.md
index bad9e0750852d99e27e4ad13e274161dace218d0..61f5babe24cd94df8acc30450bd9699bc94482e3 100644
--- a/content/2.defense-systems/rexab.md
+++ b/content/2.defense-systems/rexab.md
@@ -1,7 +1,16 @@
 ---
 title: RexAB
+tableColumns:
+    article:
+      doi: 10.1101/gad.6.3.497
+      abstract: |
+The rexA and rexB genes of bacteriophage lambda encode a two-component system that aborts lytic growth of bacterial viruses. Rex exclusion is characterized by termination of macromolecular synthesis, loss of active transport, the hydrolysis of ATP, and cell death. By analogy to colicins E1 and K, these results can be explained by depolarization of the cytoplasmic membrane. We have fractionated cells to determine the intracellular location of the RexB protein and made RexB-alkaline phosphatase fusions to analyze its membrane topology. The RexB protein appears to be a polytopic transmembrane protein. We suggest that RexB proteins form ion channels that, in response to lytic growth of bacteriophages, depolarize the cytoplasmic membrane. The Rex system requires a mechanism to prevent lambda itself from being excluded during lytic growth. We have determined that overexpression of RexB in lambda lysogens prevents the exclusion of both T4 rII mutants and lambda ren mutants. We suspect that overexpression of RexB is the basis for preventing self-exclusion following the induction of a lambda lysogen and that RexB overexpression is accomplished through transcriptional regulation.
+    Sensor: Sensing of complex phage protein/DNA
+    Activator: Direct
+    Effector: Membrane disrupting
 ---
 
+# RexAB
 ## Example of genomic structure
 
 The RexAB system is composed of 2 proteins: RexA and, RexB.
diff --git a/content/2.defense-systems/rloc.md b/content/2.defense-systems/rloc.md
index 07f8cf12182b588ba5ef3109b87c0aca818a00f5..cb72f6e818ed3988efb1461b38dd1632124a6dbd 100644
--- a/content/2.defense-systems/rloc.md
+++ b/content/2.defense-systems/rloc.md
@@ -1,7 +1,16 @@
 ---
 title: RloC
+tableColumns:
+    article:
+      doi: 10.1111/j.1365-2958.2008.06387.x
+      abstract: |
+The conserved bacterial protein RloC, a distant homologue of the tRNA(Lys) anticodon nuclease (ACNase) PrrC, is shown here to act as a wobble nucleotide-excising and Zn(++)-responsive tRNase. The more familiar PrrC is silenced by a genetically linked type I DNA restriction-modification (R-M) enzyme, activated by a phage anti-DNA restriction factor and counteracted by phage tRNA repair enzymes. RloC shares PrrC's ABC ATPase motifs and catalytic ACNase triad but features a distinct zinc-hook/coiled-coil insert that renders its ATPase domain similar to Rad50 and related DNA repair proteins. Geobacillus kaustophilus RloC expressed in Escherichia coli exhibited ACNase activity that differed from PrrC's in substrate preference and ability to excise the wobble nucleotide. The latter specificity could impede reversal by phage tRNA repair enzymes and account perhaps for RloC's more frequent occurrence. Mutagenesis and functional assays confirmed RloC's catalytic triad assignment and implicated its zinc hook in regulating the ACNase function. Unlike PrrC, RloC is rarely linked to a type I R-M system but other genomic attributes suggest their possible interaction in trans. As DNA damage alleviates type I DNA restriction, we further propose that these related perturbations prompt RloC to disable translation and thus ward off phage escaping DNA restriction during the recovery from DNA damage.
+    Sensor: Monitor the integrity of the bacterial cell machinery
+    Activator: Unknown
+    Effector: Nucleic acid degrading
 ---
 
+# RloC
 ## Example of genomic structure
 
 The RloC system is composed of one protein: RloC.
diff --git a/content/2.defense-systems/rm.md b/content/2.defense-systems/rm.md
index 159025d86cce23b9711d39b5614bef77019340a8..561087c9e577d1933013988d66fad83045b2a0eb 100644
--- a/content/2.defense-systems/rm.md
+++ b/content/2.defense-systems/rm.md
@@ -1,7 +1,16 @@
 ---
 title: RM
+tableColumns:
+    article:
+      doi: 10.1093/nar/gku734
+      abstract: |
+The roles of restriction-modification (R-M) systems in providing immunity against horizontal gene transfer (HGT) and in stabilizing mobile genetic elements (MGEs) have been much debated. However, few studies have precisely addressed the distribution of these systems in light of HGT, its mechanisms and its vectors. We analyzed the distribution of R-M systems in 2261 prokaryote genomes and found their frequency to be strongly dependent on the presence of MGEs, CRISPR-Cas systems, integrons and natural transformation. Yet R-M systems are rare in plasmids, in prophages and nearly absent from other phages. Their abundance depends on genome size for small genomes where it relates with HGT but saturates at two occurrences per genome. Chromosomal R-M systems might evolve under cycles of purifying and relaxed selection, where sequence conservation depends on the biochemical activity and complexity of the system and total gene loss is frequent. Surprisingly, analysis of 43 pan-genomes suggests that solitary R-M genes rarely arise from the degradation of R-M systems. Solitary genes are transferred by large MGEs, whereas complete systems are more frequently transferred autonomously or in small MGEs. Our results suggest means of testing the roles for R-M systems and their associations with MGEs.
+    Sensor: Detecting invading nucleic acid
+    Activator: Direct
+    Effector: Nucleic acid degrading
 ---
 
+# RM
 ## Example of genomic structure
 
 The RM system have been describe in a total of 5 subsystems.
diff --git a/content/2.defense-systems/rnlab.md b/content/2.defense-systems/rnlab.md
index fd84aa595b8df79610af2b33f165b02c2f51a23f..d504aae32aca85e223bbe05eedcadd7a2920f192 100644
--- a/content/2.defense-systems/rnlab.md
+++ b/content/2.defense-systems/rnlab.md
@@ -1,7 +1,16 @@
 ---
 title: RnlAB
+tableColumns:
+    article:
+      doi: 10.1534/genetics.110.121798
+      abstract: |
+RNase LS was originally identified as a potential antagonist of bacteriophage T4 infection. When T4 dmd is defective, RNase LS activity rapidly increases after T4 infection and cleaves T4 mRNAs to antagonize T4 reproduction. Here we show that rnlA, a structural gene of RNase LS, encodes a novel toxin, and that rnlB (formally yfjO), located immediately downstream of rnlA, encodes an antitoxin against RnlA. Ectopic expression of RnlA caused inhibition of cell growth and rapid degradation of mRNAs in ?rnlAB cells. On the other hand, RnlB neutralized these RnlA effects. Furthermore, overexpression of RnlB in wild-type cells could completely suppress the growth defect of a T4 dmd mutant, that is, excess RnlB inhibited RNase LS activity. Pull-down analysis showed a specific interaction between RnlA and RnlB. Compared to RnlA, RnlB was extremely unstable, being degraded by ClpXP and Lon proteases, and this instability may increase RNase LS activity after T4 infection. All of these results suggested that rnlA–rnlB define a new toxin–antitoxin (TA) system.
+    Sensor: Monitor the integrity of the bacterial cell machinery
+    Activator: Direct
+    Effector: Nucleic acid degrading
 ---
 
+# RnlAB
 ## Example of genomic structure
 
 The RnlAB system is composed of 2 proteins: RnlA and, RnlB.
diff --git a/content/2.defense-systems/rosmerta.md b/content/2.defense-systems/rosmerta.md
index 24b7269894c1d76635d754e76f901ef60b94ed72..3bb0979978e72fd9d3f9a34784b28259678d8f48 100644
--- a/content/2.defense-systems/rosmerta.md
+++ b/content/2.defense-systems/rosmerta.md
@@ -1,7 +1,16 @@
 ---
 title: RosmerTA
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# RosmerTA
 ## Example of genomic structure
 
 The RosmerTA system is composed of 2 proteins: RmrA_2634932349 and, RmrT_2634932349.
diff --git a/content/2.defense-systems/rst_2tm_1tm_tir.md b/content/2.defense-systems/rst_2tm_1tm_tir.md
index 3ada54e81e02fc708e7c6dd94509d537da6cd314..a3fb240a616f517a46672aa4da5fee3c569e7960 100644
--- a/content/2.defense-systems/rst_2tm_1tm_tir.md
+++ b/content/2.defense-systems/rst_2tm_1tm_tir.md
@@ -1,7 +1,13 @@
 ---
 title: Rst_2TM_1TM_TIR
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
 ---
 
+# Rst_2TM_1TM_TIR
 ## Example of genomic structure
 
 The Rst_2TM_1TM_TIR system is composed of 3 proteins: Rst_TIR_tm, Rst_1TM_TIR and, Rst_2TM_TIR.
diff --git a/content/2.defense-systems/rst_3hp.md b/content/2.defense-systems/rst_3hp.md
index 3e5012ef97a92047ac76f87f00a215ae1bafd63b..b1ffc71d9d8ca026541720efa3448f2efdd29e7e 100644
--- a/content/2.defense-systems/rst_3hp.md
+++ b/content/2.defense-systems/rst_3hp.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_3HP
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_3HP
 ## Example of genomic structure
 
 The Rst_3HP system is composed of 3 proteins: Hp1, Hp2 and, Hp3.
diff --git a/content/2.defense-systems/rst_duf4238.md b/content/2.defense-systems/rst_duf4238.md
index 5c2b0f60b396a4ab6b51fa484741556082f45bc7..c047cf372d65af43d87bfd080cd4b1892d02ce85 100644
--- a/content/2.defense-systems/rst_duf4238.md
+++ b/content/2.defense-systems/rst_duf4238.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_DUF4238
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_DUF4238
 ## Example of genomic structure
 
 The Rst_DUF4238 system is composed of one protein: DUF4238_Pers.
diff --git a/content/2.defense-systems/rst_gop_beta_cll.md b/content/2.defense-systems/rst_gop_beta_cll.md
index 51ca9ffc6cf5b3946b0c9c1a11a98e04a1cbb53a..30ff7c911a7d0b3d79dc3bac8c7f6d9f9d749bcc 100644
--- a/content/2.defense-systems/rst_gop_beta_cll.md
+++ b/content/2.defense-systems/rst_gop_beta_cll.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_gop_beta_cll
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_gop_beta_cll
 ## Example of genomic structure
 
 The Rst_gop_beta_cll system is composed of 3 proteins: gop, beta and, cll.
diff --git a/content/2.defense-systems/rst_helicaseduf2290.md b/content/2.defense-systems/rst_helicaseduf2290.md
index e813be908ff68438e3133f32197ef284d3d2b68e..844a735c1b363f461442852792f37d9a48043d7c 100644
--- a/content/2.defense-systems/rst_helicaseduf2290.md
+++ b/content/2.defense-systems/rst_helicaseduf2290.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_HelicaseDUF2290
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_HelicaseDUF2290
 ## Example of genomic structure
 
 The Rst_HelicaseDUF2290 system is composed of 2 proteins: Helicase and, DUF2290.
diff --git a/content/2.defense-systems/rst_hydrolase-3tm.md b/content/2.defense-systems/rst_hydrolase-3tm.md
index a423c687aba3555e8af37d6f7a4331e6c10c08f9..6230b566142d51ea6b05f8e54ec6eb09ffdf4f01 100644
--- a/content/2.defense-systems/rst_hydrolase-3tm.md
+++ b/content/2.defense-systems/rst_hydrolase-3tm.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_Hydrolase-3Tm
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_Hydrolase-3Tm
 ## Example of genomic structure
 
 The Rst_Hydrolase-3Tm system is composed of 2 proteins: Hydrolase and, Hydrolase-Tm.
diff --git a/content/2.defense-systems/rst_paris.md b/content/2.defense-systems/rst_paris.md
index ba76ac6be9b7e68b7c600a1c48d21eb2191d0aed..84cb5b7e78d93b9f3a955606183f85167aecddbe 100644
--- a/content/2.defense-systems/rst_paris.md
+++ b/content/2.defense-systems/rst_paris.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_PARIS
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Sensing of phage protein
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_PARIS
 ## Description
 
 PARIS (for Phage Anti-Restriction-Induced System) is a novel anti-phage system. PARIS is found in 4% of prokaryotic genomes. It comprises an ATPase associated with a DUF4435 protein, which can be found either as a two-gene cassette or a single-gene fusion (1).
diff --git a/content/2.defense-systems/rst_rt-nitrilase-tm.md b/content/2.defense-systems/rst_rt-nitrilase-tm.md
index 13a70ef02df581c448b01be0f15b45c9ba163355..737271309dcc3d2f445f663fb9dde0418c480c3a 100644
--- a/content/2.defense-systems/rst_rt-nitrilase-tm.md
+++ b/content/2.defense-systems/rst_rt-nitrilase-tm.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_RT-nitrilase-Tm
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_RT-nitrilase-Tm
 ## Example of genomic structure
 
 The Rst_RT-nitrilase-Tm system is composed of 2 proteins: RT-Tm and, RT.
diff --git a/content/2.defense-systems/rst_tir-nlr.md b/content/2.defense-systems/rst_tir-nlr.md
index 4cae46e9347d040dbdcaf6ef8ed8d3ea172c0cc5..31d7a32fa7fc4a8120094d44ffa5c3c792e2884c 100644
--- a/content/2.defense-systems/rst_tir-nlr.md
+++ b/content/2.defense-systems/rst_tir-nlr.md
@@ -1,7 +1,16 @@
 ---
 title: Rst_TIR-NLR
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.02.018
+      abstract: |
+Bacteria carry diverse genetic systems to defend against viral infection, some of which are found within prophages where they inhibit competing viruses. Phage satellites pose additional pressures on phages by hijacking key viral elements to their own benefit. Here, we show that E. coli P2-like phages and their parasitic P4-like satellites carry hotspots of genetic variation containing reservoirs of anti-phage systems. We validate the activity of diverse systems and describe PARIS, an abortive infection system triggered by a phage-encoded anti-restriction protein. Antiviral hotspots participate in inter-viral competition and shape dynamics between the bacterial host, P2-like phages, and P4-like satellites. Notably, the anti-phage activity of satellites can benefit the helper phage during competition with virulent phages, turning a parasitic relationship into a mutualistic one. Anti-phage hotspots are present across distant species and constitute a substantial source of systems that participate in the competition between mobile genetic elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Rst_TIR-NLR
 ## Example of genomic structure
 
 The Rst_TIR-NLR system is composed of one protein: TIR.
diff --git a/content/2.defense-systems/sanata.md b/content/2.defense-systems/sanata.md
index 50554264def889eab0815f2122e7eeefa2eaf466..cf1606223f7dd4e1e64275d8fe493367820fecd1 100644
--- a/content/2.defense-systems/sanata.md
+++ b/content/2.defense-systems/sanata.md
@@ -1,7 +1,16 @@
 ---
 title: SanaTA
+tableColumns:
+    article:
+      doi: 10.1016/j.molcel.2013.02.002
+      abstract: |
+Toxin-antitoxin (TA) modules, composed of a toxic protein and a counteracting antitoxin, play important roles in bacterial physiology. We examined the experimental insertion of 1.5 million genes from 388 microbial genomes into an Escherichia coli host using more than 8.5 million random clones. This revealed hundreds of genes (toxins) that could only be cloned when the neighboring gene (antitoxin) was present on the same clone. Clustering of these genes revealed TA families widespread in bacterial genomes, some of which deviate from the classical characteristics previously described for such modules. Introduction of these genes into E. coli validated that the toxin toxicity is mitigated by the antitoxin. Infection experiments with T7 phage showed that two of the new modules can provide resistance against phage. Moreover, our experiments revealed an "antidefense" protein in phage T7 that neutralizes phage resistance. Our results expose active fronts in the arms race between bacteria and phage.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# SanaTA
 ## Example of genomic structure
 
 The SanaTA system is composed of 2 proteins: SanaT and, SanaA.
diff --git a/content/2.defense-systems/sefir.md b/content/2.defense-systems/sefir.md
index e3b290bdcba975bf9dcbc9b7eb63aacca7e5ef9f..f82418c5fbef0b8974bdbfc72c078c25b74ef92d 100644
--- a/content/2.defense-systems/sefir.md
+++ b/content/2.defense-systems/sefir.md
@@ -1,7 +1,16 @@
 ---
 title: SEFIR
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# SEFIR
 ## Description
 The SEFIR defense system is composed of a single bacterial SEFIR (bSEFIR)-domain protein. bSEFIR-domain genes were identified in bacterial genomes, were shown to be enriched in defense islands and the activity of the defense system was first experimentally validated in *Bacillus sp.* NIO-1130 against phage phi29 [1]. 
 
diff --git a/content/2.defense-systems/septu.md b/content/2.defense-systems/septu.md
index 1d6735392ea42b200eabfb4262d82b33ef7c9f3b..5e7a1e195da3fca75fd57922f63a8507bfe1ddba 100644
--- a/content/2.defense-systems/septu.md
+++ b/content/2.defense-systems/septu.md
@@ -1,7 +1,16 @@
 ---
 title: Septu
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Septu
 ## Example of genomic structure
 
 The Septu system is composed of 2 proteins: PtuA and, PtuB.
diff --git a/content/2.defense-systems/shango.md b/content/2.defense-systems/shango.md
index b9c024cac0808a39e0840a616e2dc274e6949140..0ee7822f2d7ba9211e63d26b4b9d27c80ba0f508 100644
--- a/content/2.defense-systems/shango.md
+++ b/content/2.defense-systems/shango.md
@@ -1,7 +1,16 @@
 ---
 title: Shango
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Shango
 
 ## Description
 Shango is a three genes defense system which was discovered in parallel in two works in both *E.coli* and *P.aeruginosa* and was shown to have antiphage activity against the Lambda-phage in *E.coli* [1] and against diverse podo- and siphoviridae in *P.aeruginosa* [2].
diff --git a/content/2.defense-systems/shedu.md b/content/2.defense-systems/shedu.md
index 769bd62e9eea5f69a2e7250b3e41cabaea2e701e..b5a3521209fb4eab2194d5b2f7180a9fab64c07e 100644
--- a/content/2.defense-systems/shedu.md
+++ b/content/2.defense-systems/shedu.md
@@ -1,7 +1,16 @@
 ---
 title: Shedu
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Shedu
 ## Example of genomic structure
 
 The Shedu system is composed of one protein: SduA.
diff --git a/content/2.defense-systems/shosta.md b/content/2.defense-systems/shosta.md
index 7737d1fe8b137e824d6c1bca4a734b58e7d20967..2cebcd506f7ed6b0c9de8849b80986b49e1f83d7 100644
--- a/content/2.defense-systems/shosta.md
+++ b/content/2.defense-systems/shosta.md
@@ -1,7 +1,16 @@
 ---
 title: ShosTA
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# ShosTA
 ## Example of genomic structure
 
 The ShosTA system is composed of 2 proteins: ShosA and, ShosT.
diff --git a/content/2.defense-systems/sofic.md b/content/2.defense-systems/sofic.md
index 45910a14c978d4d45c019b30ef66dff2d9578e32..ac563edc901c7fa8556d305d79067c20abfb62a3 100644
--- a/content/2.defense-systems/sofic.md
+++ b/content/2.defense-systems/sofic.md
@@ -1,7 +1,16 @@
 ---
 title: SoFIC
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# SoFIC
 ## Example of genomic structure
 
 The SoFIC system is composed of one protein: SoFic.
diff --git a/content/2.defense-systems/spbk.md b/content/2.defense-systems/spbk.md
index 5be0b1477dc6bcb5255baaf1cd95cb8b064a5965..343b890a8cbedd9c7f388aa7fffba0ddcf0f165a 100644
--- a/content/2.defense-systems/spbk.md
+++ b/content/2.defense-systems/spbk.md
@@ -1,7 +1,16 @@
 ---
 title: SpbK
+tableColumns:
+    article:
+      doi: 10.1371/journal.pgen.1010065
+      abstract: |
+Most bacterial genomes contain horizontally acquired and transmissible mobile genetic elements, including temperate bacteriophages and integrative and conjugative elements. Little is known about how these elements interact and co-evolved as parts of their host genomes. In many cases, it is not known what advantages, if any, these elements provide to their bacterial hosts. Most strains of Bacillus subtilis contain the temperate phage SPß and the integrative and conjugative element ICEBs1. Here we show that the presence of ICEBs1 in cells protects populations of B. subtilis from predation by SPß, likely providing selective pressure for the maintenance of ICEBs1 in B. subtilis. A single gene in ICEBs1 (yddK, now called spbK for SPß killing) was both necessary and sufficient for this protection. spbK inhibited production of SPß, during both activation of a lysogen and following de novo infection. We found that expression spbK, together with the SPß gene yonE constitutes an abortive infection system that leads to cell death. spbK encodes a TIR (Toll-interleukin-1 receptor)-domain protein with similarity to some plant antiviral proteins and animal innate immune signaling proteins. We postulate that many uncharacterized cargo genes in ICEs may confer selective advantage to cells by protecting against other mobile elements.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# SpbK
 ## Example of genomic structure
 
 The SpbK system is composed of one protein: SpbK.
diff --git a/content/2.defense-systems/sspbcde.md b/content/2.defense-systems/sspbcde.md
index f8e7de76f9aadb510de643459a8b48d8835dc581..7631a766b94a7666f18f4a90a44dd7ed2ac737e6 100644
--- a/content/2.defense-systems/sspbcde.md
+++ b/content/2.defense-systems/sspbcde.md
@@ -1,7 +1,16 @@
 ---
 title: SspBCDE
+tableColumns:
+    article:
+      doi: 10.1128/mBio.00613-21
+      abstract: |
+Unlike nucleobase modifications in canonical restriction-modification systems, DNA phosphorothioate (PT) epigenetic modification occurs in the DNA sugar-phosphate backbone when the nonbridging oxygen is replaced by sulfur in a double-stranded (ds) or single-stranded (ss) manner governed by DndABCDE or SspABCD, respectively. SspABCD coupled with SspE constitutes a defense barrier in which SspE depends on sequence-specific PT modifications to exert its antiphage activity. Here, we identified a new type of ssDNA PT-based SspABCD-SspFGH defense system capable of providing protection against phages through a mode of action different from that of SspABCD-SspE. We provide further evidence that SspFGH damages non-PT-modified DNA and exerts antiphage activity by suppressing phage DNA replication. Despite their different defense mechanisms, SspFGH and SspE are compatible and pair simultaneously with one SspABCD module, greatly enhancing the protection against phages. Together with the observation that the sspBCD-sspFGH cassette is widely distributed in bacterial genomes, this study highlights the diversity of PT-based defense barriers and expands our knowledge of the arsenal of phage defense mechanisms.IMPORTANCE We recently found that SspABCD, catalyzing single-stranded (ss) DNA phosphorothioate (PT) modification, coupled with SspE provides protection against phage infection. SspE performs both PT-simulated NTPase and DNA-nicking nuclease activities to damage phage DNA, rendering SspA-E a PT-sensing defense system. To our surprise, ssDNA PT modification can also pair with a newly identified 3-gene sspFGH cassette to fend off phage infection with a different mode of action from that of SspE. Interestingly, both SspFGH and SspE can pair with the same SspABCD module for antiphage defense, and their combination provides Escherichia coli JM109 with additive phage resistance up to 105-fold compared to that for either barrier alone. This agrees with our observation that SspFGH and SspE coexist in 36 bacterial genomes, highlighting the diversity of the gene contents and molecular mechanisms of PT-based defense systems.
+    Sensor: Detecting invading nucleic acid
+    Activator: Direct
+    Effector: Nucleic acid degrading
 ---
 
+# SspBCDE
 ## Example of genomic structure
 
 The SspBCDE system is composed of 7 proteins: SspB, SspC, SspD, SspE, SspH, SspG and, SspF.
diff --git a/content/2.defense-systems/stk2.md b/content/2.defense-systems/stk2.md
index a01db5db00121b583ec0a9bd4a9dd94da8c66ef3..06c4ebe4806498359b9f6f5d2a2c1a9a214b92ab 100644
--- a/content/2.defense-systems/stk2.md
+++ b/content/2.defense-systems/stk2.md
@@ -1,7 +1,16 @@
 ---
 title: Stk2
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2016.08.010
+      abstract: |
+Organisms from all domains of life are infected by viruses. In eukaryotes, serine/threonine kinases play a central role in antiviral response. Bacteria, however, are not commonly known to use protein phosphorylation as part of their defense against phages. Here we identify Stk2, a staphylococcal serine/threonine kinase that provides efficient immunity against bacteriophages by inducing abortive infection. A phage protein of unknown function activates the Stk2 kinase. This leads to the Stk2-dependent phosphorylation of several proteins involved in translation, global transcription control, cell-cycle control, stress response, DNA topology, DNA repair, and central metabolism. Bacterial host cells die as a consequence of Stk2 activation, thereby preventing propagation of the phage to the rest of the bacterial population. Our work shows that mechanisms of viral defense that rely on protein phosphorylation constitute a conserved antiviral strategy across multiple domains of life.
+    Sensor: Sensing of phage protein
+    Activator: Direct
+    Effector: Other (protein modifying)
 ---
 
+# Stk2
 ## Description
 
 Eukaryotic-like serine/threonine kinases have a variety of functions in prokaryotes. Recently, a single-gene system (Stk2) encoding for a Serine/threonine kinase from Staphylococcus epidermidis has been found to have anti-phage activity both in its native host and in a heterologous S.aureus host (Depardieu et al., 2016). 
diff --git a/content/2.defense-systems/thoeris.md b/content/2.defense-systems/thoeris.md
index f43c233e88ec60036cff1ecb0bf232865d1025e7..aa70dbc4273536f0a8000e9988e1361017a50c23 100644
--- a/content/2.defense-systems/thoeris.md
+++ b/content/2.defense-systems/thoeris.md
@@ -1,7 +1,16 @@
 ---
 title: Thoeris
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Signaling
+    Effector: Nucleotide modifying
 ---
 
+# Thoeris
 ## Example of genomic structure
 
 The Thoeris system have been describe in a total of 2 subsystems.
diff --git a/content/2.defense-systems/tiamat.md b/content/2.defense-systems/tiamat.md
index f23636a97d9ea8cc8ac8123d556c1927e87e9fd0..d28fe44034314c063e37e8d9c7b24190294e4f6a 100644
--- a/content/2.defense-systems/tiamat.md
+++ b/content/2.defense-systems/tiamat.md
@@ -1,7 +1,16 @@
 ---
 title: Tiamat
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Tiamat
 ## Example of genomic structure
 
 The Tiamat system is composed of one protein: TmtA_2599863134.
diff --git a/content/2.defense-systems/uzume.md b/content/2.defense-systems/uzume.md
index d2c63541176a1fd979ab7f5f4560610552bcfc2f..b63d11f557c6b51f18ea6daaee1ce6e7f46facad 100644
--- a/content/2.defense-systems/uzume.md
+++ b/content/2.defense-systems/uzume.md
@@ -1,7 +1,16 @@
 ---
 title: Uzume
+tableColumns:
+    article:
+      doi: 10.1016/j.chom.2022.09.017
+      abstract: |
+Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments. We identified multiple systems with domains involved in eukaryotic antiviral immunity, including those homologous to the ubiquitin-like ISG15 protein, dynamin-like domains, and SEFIR domains, and show their participation in bacterial defenses. Additional systems include domains predicted to manipulate DNA and RNA molecules, alongside toxin-antitoxin systems shown here to function in anti-phage defense. These systems are widely distributed in microbial genomes, and in some bacteria, they form a considerable fraction of the immune arsenal. Our data substantially expand the inventory of defense systems utilized by bacteria to counteract phage infection.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Uzume
 ## Example of genomic structure
 
 The Uzume system is composed of one protein: UzuA_2660320622.
diff --git a/content/2.defense-systems/viperin.md b/content/2.defense-systems/viperin.md
index d0cd5e2b9355c478168900e3317137c60e748485..04b98ff64931956cd8970533539140a2b78c0c78 100644
--- a/content/2.defense-systems/viperin.md
+++ b/content/2.defense-systems/viperin.md
@@ -1,7 +1,16 @@
 ---
 title: Viperin
+tableColumns:
+    article:
+      doi: 10.1038/s41586-020-2762-2
+      abstract: |
+Viperin is an interferon-induced cellular protein that is conserved in animals1. It has previously been shown to inhibit the replication of multiple viruses by producing the ribonucleotide 3?-deoxy-3?,4?-didehydro (ddh)-cytidine triphosphate (ddhCTP), which acts as a chain terminator for viral RNA polymerase2. Here we show that eukaryotic viperin originated from a clade of bacterial and archaeal proteins that protect against phage infection. Prokaryotic viperins produce a set of modified ribonucleotides that include ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). We further show that prokaryotic viperins protect against T7 phage infection by inhibiting viral polymerase-dependent transcription, suggesting that it has an antiviral mechanism of action similar to that of animal viperin. Our results reveal a class of potential natural antiviral compounds produced by bacterial immune systems.
+    Sensor: Unknown
+    Activator: Direct
+    Effector: Nucleotide modifying
 ---
 
+# Viperin
 ## Description
  
 Viperins, for “Virus Inhibitory Protein, Endoplasmic Reticulum-associated, INterferon-inducible”, are antiviral enzymes whose expression is stimulated by interferons in eukaryotic cells. They are important components of eukaryotic innate immunity, and present antiviral activity against a wide diversity of viruses, including double-stranded DNA viruses, single-strand RNA viruses and retroviruses (1).  
diff --git a/content/2.defense-systems/wadjet.md b/content/2.defense-systems/wadjet.md
index 024f7a9c514520ee86149b28aa5570e7b8e44e0c..dda8c225df8cb2a6dd668c28c3c9ca616e75f8de 100644
--- a/content/2.defense-systems/wadjet.md
+++ b/content/2.defense-systems/wadjet.md
@@ -1,7 +1,16 @@
 ---
 title: Wadjet
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Detecting invading nucleic acid
+    Activator: Direct
+    Effector: Nucleic acid degrading
 ---
 
+# Wadjet
 ## Example of genomic structure
 
 The Wadjet system have been describe in a total of 4 subsystems.
diff --git a/content/2.defense-systems/zorya.md b/content/2.defense-systems/zorya.md
index 28c37942d06e3b6bb450651d665598319f0113d0..09607924655cd864e0a127a63c5ee6491144f049 100644
--- a/content/2.defense-systems/zorya.md
+++ b/content/2.defense-systems/zorya.md
@@ -1,7 +1,16 @@
 ---
 title: Zorya
+tableColumns:
+    article:
+      doi: 10.1126/science.aar4120
+      abstract: |
+The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
+    Sensor: Unknown
+    Activator: Unknown
+    Effector: Unknown
 ---
 
+# Zorya
 ## Example of genomic structure
 
 The Zorya system have been describe in a total of 2 subsystems.