diff --git a/components/content/StructureDb.vue b/components/content/StructureDb.vue
index 6fc5a9c846bd0f171f139c6712b8074eef3fe48e..34e6693631d10322d0e3c19b886fad4eddd952f0 100644
--- a/components/content/StructureDb.vue
+++ b/components/content/StructureDb.vue
@@ -5,7 +5,7 @@ import type { SortItem } from "@/components/ServerDbTable.vue"
import { ServerDbTable } from "#components"
const sortBy: Ref<SortItem[]> = ref([{ key: 'system', order: "asc" }])
const itemValue = ref("id");
-const facets: Ref<string[]> = ref(["system", "completed", "prediction_type", ])
+const facets: Ref<string[]> = ref(["system", "completed", "prediction_type",])
const headers: Ref<Object[]> = ref([
{ title: 'Structure', key: 'structure', sortable: false, removable: false },
{ title: "Type", key: "system", removable: false },
@@ -56,7 +56,14 @@ function pdbNameToCif(pdbPath: string) {
function toSystemName(rawName: string) {
- return rawName.split(/_|-0/)[0].toLocaleLowerCase()
+ // split on -0 if exists else on _
+ if (rawName.includes("-0")) {
+
+ return rawName.split("-0")[0].toLocaleLowerCase()
+ } else {
+ return rawName.split("_")[0].toLocaleLowerCase()
+ }
+
}
diff --git a/content/2.general-concepts/5.defense-systems-discovery.md b/content/2.general-concepts/5.defense-systems-discovery.md
index c5a661a2252bb6baba9aa827e994fb50c7cfbb85..1347fd5217f1878db49bc9f0a30c854d149fae0c 100644
--- a/content/2.general-concepts/5.defense-systems-discovery.md
+++ b/content/2.general-concepts/5.defense-systems-discovery.md
@@ -2,6 +2,15 @@
title: Discovery of defense systems
layout: article
toc: true
+contributors:
+ - Helena Shomar
---
-Defense systems are known since the birth of molecular biology. Then, more were discovered.
+# Discovery of defense systems
+
+Anti-phage defense systems have been discovered through various research methodologies and scientific investigations.
+
+The first defense systems that were discovered and characterized were restriction modifications (RM) and CRISPR-cas systems, in the 1960s and early 2000s respectively. These systems are the most abundantly encoded in prokaryotic genomes and were discovered by researchers that observed heritable bacterial resistance of certain strains to bacteriophages. A combination of functional studies, bacterial genetics, and biochemical assays enabled to elucidate their mechanisms of action, leading to the development of tools that revolutionized molecular biology and genetic engineering.
+
+In recent years, the discovery and characterization of dozens of novel anti-phage defense systems involve a combination of bioinformatics, genomics analysis and experimental approaches. The computational pipeline that has allowed to identify and validate numerous systems in the past years is based on the observation that anti-phage defense systems tend to co-localize on prokaryotic chromosomes in regions denoted as defense islands. Using this principle, recent studies have discovered more than 150 novel systems, by identifying and testing single or multi protein uncharacterized systems that are enriched within such defense islands. Candidate systems are typically cloned into heterologous expression hosts, to validate their anti-phage function. The mechanisms of many these newly discovered systems remain unknown.
+
diff --git a/content/2.general-concepts/7.mge-defense-systems.md b/content/2.general-concepts/7.mge-defense-systems.md
index 616f781c16265c04e5941b0995e9a9d430e9e30c..634fc571d8fca3118e1c13e719cc6f3409bbb25c 100644
--- a/content/2.general-concepts/7.mge-defense-systems.md
+++ b/content/2.general-concepts/7.mge-defense-systems.md
@@ -1,7 +1,8 @@
---
title: Defense Systems and MGE
-layout: article-no-toc
+contributors:
+ - Marian Dominguez-Mirazo
+layout: article
---
-Defense systems help bacteria against mobile genetic elements (MGE), such as phage or plasmids.
-Yet, some defense systems favor certain MGE, or some MGE carry defense systems.
\ No newline at end of file
+Mobile genetic elements (MGEs), such as plasmids, bacteriophages, and phage satellites, facilitate horizontal gene transfer (HGT) within microbial populations, playing a crucial role in the genetic diversity and genomic evolution of bacteria :ref{doi=10.1098/rstb.2020.0460}. These elements expedite the exchange of genetic material among bacterial cells, promoting the dissemination of advantageous traits like antibiotic resistance, virulence factors, and metabolic capabilities, allowing bacteria to adapt to dynamic environments :ref{doi=10.1098/rstb.2020.0460}. However, the presence of MGEs can impose a substantial fitness cost on the bacterial host, as in the case of lytic phage infections. To counteract parasitic genomic elements, including viruses and other MGEs, bacteria have evolved defense systems. These defense systems are often disadvantageous under low parasite pressure, leading to their occasional loss. However, as the pressure from parasites increases, these defense systems become advantageous. Consequently, defense systems in bacteria exhibit high mobility and transfer rates :ref{doi=10.1038/s41576-019-0172-9}. Interestingly, a large fraction of defense systems in bacteria are encoded by MGEs :ref{doi=10.1038/s41467-022-30269-9,10.1371/journal.pbio.3001514}. While sometimes the fitness interests of MGEs and the bacterial host are aligned, these systems are likely to be selected because they benefit the MGE encoding it rather than the host cell who :ref{doi=10.1371/journal.pbio.3001514,10.1038/s41576-019-0172-9}. This benefit may include preventing other mobile elements from infecting the same cell and competing for essential resources. The presence of defense systems can, in turn, have an effect in gene flow who :ref{doi=10.1371/journal.pbio.3001514}.
diff --git a/content/3.defense-systems/abih.md b/content/3.defense-systems/abih.md
index d85ace09e30015fdf10fa4652b0e79937e5ea43f..475a4ffd9b910d0ec2db566c1f209ddf26bd5f8e 100644
--- a/content/3.defense-systems/abih.md
+++ b/content/3.defense-systems/abih.md
@@ -18,6 +18,13 @@ relevantAbstracts:
---
# AbiH
+
+## Description
+AbiH is a single-gene abortive infection system described in Lactococcus.
+
+## Molecular mechanism
+To the best of our knowledge, no molecular mechanism has been described so far for AbiH.
+
## Example of genomic structure
The AbiH is composed of 1 protein: AbiH.
diff --git a/content/3.defense-systems/card_nlr.md b/content/3.defense-systems/card_nlr.md
index 37a33fce5a41f39aa18e2a57d24e65af762a546b..ea80ff9028681e5a459b91290d4d70ac045fbb74 100644
--- a/content/3.defense-systems/card_nlr.md
+++ b/content/3.defense-systems/card_nlr.md
@@ -6,12 +6,22 @@ tableColumns:
doi: 10.1101/2023.05.28.542683
abstract: |
Caspase recruitment domains (CARDs) and pyrin domains are important facilitators of inflammasome activity and pyroptosis. Upon pathogen recognition by NLR proteins, CARDs recruit and activate caspases, which, in turn, activate gasdermin pore forming proteins to and induce pyroptotic cell death. Here we show that CARD-like domains are present in defense systems that protect bacteria against phage. The bacterial CARD is essential for protease-mediated activation of certain bacterial gasdermins, which promote cell death once phage infection is recognized. We further show that multiple anti-phage defense systems utilize CARD-like domains to activate a variety of cell death effectors. We find that these systems are triggered by a conserved immune evasion protein that phages use to overcome the bacterial defense system RexAB, demonstrating that phage proteins inhibiting one defense system can activate another. We also detect a phage protein with a predicted CARD-like structure that can inhibit the CARD-containing bacterial gasdermin system. Our results suggest that CARD domains represent an ancient component of innate immune systems conserved from bacteria to humans, and that CARD-dependent activation of gasdermins is conserved in organisms across the tree of life.
+ Sensor: Unknown
+ Activator: Unknown
+ Effector: Membrane disrupting or other
PFAM: PF00082, PF00089, PF00614, PF01223, PF13091, PF13191, PF13365
+contributors:
+ - Marian Dominguez-Mirazo
+relevantAbstract:
+ - doi: 10.1101/2023.05.28.542683
---
# CARD_NLR
+## Description
+Pore-forming proteins called gasdermins control cell-death response to infection in animals. Gasdermins are also present in bacteria where they have been shown to act as an abortive infection system that permeabilizes the cell membrane before phage release :ref{doi=10.1126/science.abj8432,10.1101/2023.05.28.542683}. In *Lysobacter*, the gasdermin operon includes two genes encoding trypsin-like protease domains, and a gene encoding an ATPase domain :ref{doi=10.1101/2023.05.28.542683}. Intact active sites for the second protease and the ATPase, but not the first protease, are required for succesful phage defense :ref{doi=10.1126/science.abj8432}. The domain architecture of the ATPase suggests it belongs to a protein family that is considered the ancestor of the eukaryotic nucleotide oligomerization domain (NOD)-like receptor (NLR) protein family :ref{doi=10.1101/2023.05.28.542683}. In animals, NLR initiates the formation of the inflammasome complex :ref{doi=10.1126/science.abe3069}. The second protease contains a region with similar structure to human CARD domain :ref{doi=10.1101/2023.05.28.542683}. The CARD domain takes part on the assembly of immune protein complexes :ref{doi=10.1038/sj.cdd.4401890}. The CARD-like domain in the *Lysobacter* system is required for succesful phage defense :ref{doi=10.1101/2023.05.28.542683}. Homology searches recovered multiple bacterial operons that include two proteases, one of them containing a CARD-like domain, and a NLR-like protein. In most cases, the effector gasdermin gene was replaced by another gene:ref{doi=10.1101/2023.05.28.542683}. The operon found in *Pedobacter rhizosphaerae* exhibits phage defense capabilities and contains a protein with phospholipase and endonuclease domains replacing the gasdermin gene. This system confers protection against the same phages as the *Lysobacter* gasdermin containing system, suggesting that the proteases and ATPase participate in phage specificity and recognition.
-## To do
+## Molecular mechanisms
+For the *Lysobacter* system, the effector has been described as a pore-formin protein that disrupts the cell membrane :ref{doi=10.1101/2023.05.28.542683}. To our knowledge, other parts of the molecular mechanisms have yet to be elucidated.
## Example of genomic structure
@@ -49,13 +59,3 @@ The system was detected in 57 different species.
Proportion of genome encoding the CARD_NLR system for the 14 phyla with more than 50 genomes in the RefSeq database.
-
-## Relevant abstract
-::relevant-abstracts
----
-items:
- - doi: 10.1101/2023.05.28.542683
-
----
-::
-
diff --git a/content/3.defense-systems/fs_hp.md b/content/3.defense-systems/fs_hp.md
index 34e1a5b53ab0552d143758e7bcb96a293e7213aa..b256ce11251b3d89348f2d319e33f6fe6c670d37 100644
--- a/content/3.defense-systems/fs_hp.md
+++ b/content/3.defense-systems/fs_hp.md
@@ -6,11 +6,21 @@ tableColumns:
doi: 10.1016/j.cell.2022.07.014
abstract: |
Bacteria encode sophisticated anti-phage systems that are diverse and versatile and display high genetic mobility. How this variability and mobility occurs remains largely unknown. Here, we demonstrate that a widespread family of pathogenicity islands, the phage-inducible chromosomal islands (PICIs), carry an impressive arsenal of defense mechanisms, which can be disseminated intra- and inter-generically by helper phages. These defense systems provide broad immunity, blocking not only phage reproduction, but also plasmid and non-cognate PICI transfer. Our results demonstrate that phages can mobilize PICI-encoded immunity systems to use them against other mobile genetic elements, which compete with the phages for the same bacterial hosts. Therefore, despite the cost, mobilization of PICIs may be beneficial for phages, PICIs, and bacteria in nature. Our results suggest that PICIs are important players controlling horizontal gene transfer and that PICIs and phages establish mutualistic interactions that drive bacterial ecology and evolution.
+ Sensor: Unknown
+ Activator: Unknown
+ Effector: Unknown
+contributors:
+ - Marian Dominguez-Mirazo
+relevantAbstracts:
+ - doi: 10.1016/j.cell.2022.07.014
---
# FS_HP
-## To do
+## Description
+PICIs (Phage-inducible chromosomal islands) are highly mobile genetic elements that reside in the bacterial chromosome in the absence of a helper phage. Following infection by the helper phage, PICIs excise and replicate by hijacking the helper phage machinery. The FS_HP system was discovered in E. fergusonii through manual search for immune systems in flanking regions of gram-negative PICIs :ref{doi=10.1016/j.cell.2022.07.014}. It is composed by a single protein with a hypothetical domain, from which it derives the HP part of its name. The system showcases a broad defense spectrum. It was tested against 15 lytic phages in 3 gram negative bacteria, and protected the bacterial host against 3 unrelated phages in 2 different bacteria species. FS_HP also blocked the formation of phage particles upon induction of the P22 S. enterica prophage. Therefore, the system can block phage in both lytic and lysogenic life cycles. It was also shown to reduce the production of transducing particles.
+## Molecular mechanisms
+As far as we are aware, the molecular mechanism is unknown.
## Example of genomic structure
@@ -76,11 +86,3 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
-## Relevant abstract
-::relevant-abstracts
----
-items:
- - doi: 10.1016/j.cell.2022.07.014
-
----
-::
diff --git a/content/3.defense-systems/gaps1.md b/content/3.defense-systems/gaps1.md
index d8e61a14fb673cf7bc16930ea38a6f225cfdd8a8..c7eb1ed59a5c3cd8a85b38f9df9218ec9cb85895 100644
--- a/content/3.defense-systems/gaps1.md
+++ b/content/3.defense-systems/gaps1.md
@@ -6,11 +6,23 @@ tableColumns:
doi: 10.1101/2023.03.28.534373
abstract: |
Bacteria are found in ongoing conflicts with rivals and predators, which lead to an evolutionary arms race and the development of innate and adaptive immune systems. Although diverse bacterial immunity mechanisms have been recently identified, many remain unknown, and their dissemination within bacterial populations is poorly understood. Here, we describe a widespread genetic element, defined by the Gamma-Mobile-Trio (GMT) proteins, that serves as a mobile bacterial weapons armory. We show that GMT islands have cargo comprising various combinations of secreted antibacterial toxins, anti-phage defense systems, and secreted anti-eukaryotic toxins. This finding led us to identify four new anti-phage defense systems encoded within GMT islands and reveal their active domains and mechanisms of action. We also find the phage protein that triggers the activation of one of these systems. Thus, we can identify novel toxins and defense systems by investigating proteins of unknown function encoded within GMT islands. Our findings imply that the concept of "defense islands" may be broadened to include other types of bacterial innate immunity mechanisms, such as antibacterial and anti-eukaryotic toxins that appear to stockpile with anti-phage defense systems within GMT weapon islands.
+ Sensor: Phage-protein sensing
+ Activator: Unknown
+ Effector: Unknown
+contributors:
+ - Marian Dominguez-Mirazo
+relevantAbstracts:
+ - doi: 10.1101/2023.03.28.534373
---
# GAPS1
-## To do
+## Description
+The GAPS1 system is composed of a single protein. It was found in Gamma-Mobile-Trio (GMT) protein containing genomic island in *Vibrio*, and cloned into *E. coli* K-12 :ref{doi=10.1101/2023.03.28.534373}. The name GAPS derives from the "GMT-encoded Anti-Phage System" acronym. GAPS1 contains a predicted nuclease domain whose mutation prevents defense activity, however DNA degradation was not detected in targeted phage :ref{doi=10.1101/2023.03.28.534373}. Mutations in the folded capsid protein (Gp10) of phage T7 result in a escape phenotype, with GAPS1 shown to be activated upon Gp10 expression, suggesting activation of the system at late stages of the infection cycle :ref{doi=10.1101/2023.03.28.534373}.
+
+## Molecular mechanisms
+The molecular mechanism remains to be fully elucidated.
+
## Example of genomic structure
@@ -69,11 +81,4 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
-## Relevant abstract
-::relevant-abstracts
----
-items:
- - doi: 10.1101/2023.03.28.534373
----
-::
diff --git a/content/3.defense-systems/lamassu-fam.md b/content/3.defense-systems/lamassu-fam.md
index cadf37d464206fd054fa6307154d5269702079ac..3fcb7cea7856512f76dfc66ed9b81933e4facc9b 100644
--- a/content/3.defense-systems/lamassu-fam.md
+++ b/content/3.defense-systems/lamassu-fam.md
@@ -9,21 +9,32 @@ tableColumns:
Sensor: Unknown
Activator: Unknown
Effector: Diverse (Nucleic acid degrading (?), Nucleotide modifying (?), Membrane disrupting (?))
- PFAM: PF00753, PF02463, PF05057, PF12532, PF13175, PF13289, PF13476, PF14130
+ PFAM: PF00753, PF02463, PF05057, PF12532, PF13175, PF13289, PF13476, PF14130
+contributors:
+ - Matthieu Haudiquet
+ - Aude Bernheim
+relevantAbstracts:
+ - doi: 10.1126/science.aar4120
+ - doi: 10.1016/j.chom.2022.09.017
+ - doi: 10.1093/nar/gkab883
+ - doi: 10.1038/s41586-022-04546-y
+ - doi: 10.1101/2022.11.18.517080
---
# 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. Â
+The original types of Lamassu systems are Lamassu Type 1 :ref{doi=10.1126/science.aar4120} and Type 2 :ref{doi=10.1016/j.chom.2022.09.017}. They both necessarily comprise two genes *lmuA* and *lmuB*, to which a third gene (*lmuC*) is added in the case of Lamassu Type 2. Â
-More recently, Lamassu has been suggested to be a large family of defense systems, that can be classified into multiple subtypes.Â
+Lamassu has been suggested to be a large family of defense systems, that can be classified into multiple subtypes :ref{doi=10.1016/j.chom.2022.09.017}.Â
-These systems all encode the *lmuB* gene, and in most cases also comprise *lmuC.* In addition to these two core genes, Lamassu systems of various subtypes encode a third protein, hypothesized to be the Abi effector protein (3). This effector  can not only be LmuA (Lamassu Type1 and 2) but also proteins encoding endonuclease domains, SIR2-domains, or even hydrolase domains (3). Systems of the extended Lamassu-family can be found in 10% of prokaryotic genomes (3).
+These systems all encode the *lmuB* gene, and in most cases also comprise *lmuC*. In addition to these two core genes, Lamassu systems of various subtypes encode a third protein, hypothesized to be the Abi effector protein :ref{doi=10.1101/2022.05.11.491447}. This effector  can be proteins encoding endonuclease domains, SIR2-domains, or even hydrolase domains :ref{doi=10.1016/j.chom.2022.09.017}. Systems of the extended Lamassu-family can be found in 10% of prokaryotic genomes :ref{doi=10.1016/j.chom.2022.09.017}.
+
+Lamassu were also described as DdmABC in *Vibrio cholerae* :ref{doi=10.1038/s41586-022-04546-y,10.1101/2022.11.18.517080}. They were found to be antiplasmids and thus to eliminate plasmids from seventh pandemic *Vibrio cholerae* :ref{doi=10.1038/s41586-022-04546-y}.
## Molecular mechanism
-Lamassu systems function through abortive infection (Abi), but their molecular mechanism remains to be described.
+Lamassu systems function through abortive infection (Abi), but the molecular mechanism remains to be described. It was shown that, in Vibrio cholerae palindromic DNA sequences that are predicted to form stem-loop hairpin trigger the system :ref{doi=10.1101/2022.11.18.517080}.
## Example of genomic structure
@@ -426,24 +437,3 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
- - doi: 10.1016/j.chom.2022.09.017
- - doi: 10.1038/s41586-022-04546-y
- - doi: 10.1126/science.aar4120
-
----
-::
-
-
-## References
-
-1. Doron S, Melamed S, Ofir G, et al. Systematic discovery of antiphage defense systems in the microbial pangenome. *Science*. 2018;359(6379):eaar4120. doi:10.1126/science.aar4120
-
-2. Payne LJ, Todeschini TC, Wu Y, et al. Identification and classification of antiviral defence systems in bacteria and archaea with PADLOC reveals new system types. *Nucleic Acids Res*. 2021;49(19):10868-10878. doi:10.1093/nar/gkab883
-
-3. Millman, A., Melamed, S., Leavitt, A., Doron, S., Bernheim, A., Hör, J., Lopatina, A., Ofir, G., Hochhauser, D., Stokar-Avihail, A., Tal, N., Sharir, S., Voichek, M., Erez, Z., Ferrer, J.L.M., Dar, D., Kacen, A., Amitai, G., Sorek, R., 2022. An expanding arsenal of immune systems that protect bacteria from phages. bioRxiv. https://doi.org/10.1101/2022.05.11.491447
-
diff --git a/content/3.defense-systems/mmb_gp29_gp30.md b/content/3.defense-systems/mmb_gp29_gp30.md
index fe3a9d9500be6cbbd71f32a9aab63abeea250d3d..1669c5f9dc9c4be30718e680a02da41f78cd523c 100644
--- a/content/3.defense-systems/mmb_gp29_gp30.md
+++ b/content/3.defense-systems/mmb_gp29_gp30.md
@@ -6,11 +6,19 @@ tableColumns:
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.
+contributors:
+ - Hugo Vaysset
+relevantAbstract:
+ - 10.1038/nmicrobiol.2016.251
---
-# MMB_gp29_gp30
+# MMB gp29-gp30
-## To do
+## Description
+MMB gp29-gp30 is a defense system which was in the MichelleMyBell (MMB) temperate mycobacteriophage. It is an example of prophage-mediated defense :ref{doi=10.1038/nmicrobiol.2016.251}.
+
+## Molecular mechanisms
+To the extent of our knowledge, the precise mechanism of action of MMB gp29-gp30 is not known. The system was shown to protect against lytic infection by temperate phage (e.g. phage Tweety) and does not act through abotive infection. Cells that survive infection tend to become lysogens for the infecting phage. It was also shown that the expression of gp29 alone was toxic in *M. smegmatis* :ref{doi=10.1038/nmicrobiol.2016.251}.
## Example of genomic structure
@@ -77,11 +85,3 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
-## Relevant abstract
-::relevant-abstracts
----
-items:
- - doi: 10.1038/nmicrobiol.2016.251
-
----
-::
diff --git a/content/3.defense-systems/shosta.md b/content/3.defense-systems/shosta.md
index 9ad8cab412ed6b9eb855bb917ce0d723c18ae646..934c4230cbcdece5057a080b56fc7642bb6acbde 100644
--- a/content/3.defense-systems/shosta.md
+++ b/content/3.defense-systems/shosta.md
@@ -10,9 +10,23 @@ tableColumns:
Activator: Unknown
Effector: Unknown
PFAM: PF02481
+relevantAbstracts:
+ - doi: 10.1016/j.chom.2022.09.017
+ - doi: 10.1016/j.chom.2022.02.018
+ - doi: 10.1101/gr.133850.111
---
# ShosTA
+
+## Description
+
+ShosTA system was first described as a Toxin/Antitoxin system in 2012 :ref{doi=10.1101/gr.133850.111} without demonstration of antiphage activity. In 2022, a paper described the same system as "DprA + PRTase" inside P2 like prophages and prooves its antiphage activity. Finally, the antiphage activity was also prooved in another study with the original name ShosTA :ref{doi=10.1016/j.chom.2022.09.017}.
+
+This system is composed of two protein: ShosT and ShosA encoding for Hydrolase/PRTase and DprA (nucleotid binding) respectively.
+
+## Molecular mechanism
+The ShosTA system is a toxin (ShosT) antitoxin (ShosA) system. The domains of ShosT (Hydrolase and PRTase) allows us to hypothesize a toxicity linked to host protein degradation.
+
## Example of genomic structure
The ShosTA is composed of 2 proteins: ShosA and ShosT.
@@ -88,15 +102,5 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
-## Relevant abstracts
-::relevant-abstracts
----
-items:
- - doi: 10.1016/j.chom.2022.09.017
- - doi: 10.1016/j.chom.2022.09.017
- - doi: 10.1101/gr.133850.111
-
----
-::