From 5f0fd770811e14d0f6c0def60f55a34073583972 Mon Sep 17 00:00:00 2001
From: Jean CURY <jean.cury@pasteur.fr>
Date: Fri, 15 Dec 2023 16:50:14 +0100
Subject: [PATCH] Update card_nlr.md
---
content/3.defense-systems/card_nlr.md | 6 +++++-
1 file changed, 5 insertions(+), 1 deletion(-)
diff --git a/content/3.defense-systems/card_nlr.md b/content/3.defense-systems/card_nlr.md
index 00fc5935..dda428e0 100644
--- a/content/3.defense-systems/card_nlr.md
+++ b/content/3.defense-systems/card_nlr.md
@@ -10,6 +10,10 @@ tableColumns:
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
@@ -17,7 +21,7 @@ tableColumns:
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.
## 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 out knowledge, other parts of the molecular mechanisms have yet to be elucidated.
+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
--
GitLab