Merge branch 'hgeorjon-main-patch-80781' into 'main'

Update nlr.md (issue #214)

See merge request !78

content/3.defense-systems/nlr.md

@@ -3,18 +3,33 @@ title: NLR
 layout: article
 tableColumns:
     article:
-      doi: 10.1101/2022.07.19.500537
+      doi: 10.1016/j.cell.2023.04.015
       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.
+        Bacteria use a wide range of immune pathways to counter phage infection. A subset of these genes shares 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 the 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
     PFAM: PF05729
-relevantAbstracts:
-    - doi: 10.1101/2022.07.19.500537
+contributors:
+    - Héloïse Georjon
+relevantAbstract:
+    - doi: 10.1016/j.cell.2023.04.015
 ---
 
-# NLR
+# NLR / bNACHT
+## Description
+This NLR like system is also known as the bNACHT systems.
+
+Several proteins containing a NACHT module were found to have anti-phage activity. NACHT modules are also found in metazoans, where they play a role in innate immunity. 
+
+bNacht systems have some similarities with other defense systems:
+[CARD_NLR](/defense-systems/card_nlr) , [Rst_TIR-NLR](/defense-systems/rst_tir-nlr), [Avs](/defense-systems/avs).
+
+## Molecular mechanism
+
+Bacterial NACHT module-containing proteins (bNACHT) encompass a C-terminal sensor, a central NACHT module, and N-terminal effector modules. The N-terminal effectors associated with bNACHT proteins are diverse, and include domains that have been previously described to be involved in other defense systems {doi=10.1016/j.cell.2023.04.015}
+As far as we are aware, the precise molecular mechanism of bNACHT is unknown.
+
 ## Example of genomic structure
 
 A total of 2 subsystems have been described for the NLR system.
@@ -179,3 +194,5 @@ end
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+::
+