From 4845d78302f59b82445a61e3d020c095bd5a150f Mon Sep 17 00:00:00 2001
From: Lucas PAOLI <lucas.paoli@pasteur.fr>
Date: Wed, 22 Nov 2023 18:04:33 +0100
Subject: [PATCH] Add missing abstract
---
content/3.defense-systems/dgtpase.md | 6 ++++--
1 file changed, 4 insertions(+), 2 deletions(-)
diff --git a/content/3.defense-systems/dgtpase.md b/content/3.defense-systems/dgtpase.md
index 5579266d..a60abd95 100644
--- a/content/3.defense-systems/dgtpase.md
+++ b/content/3.defense-systems/dgtpase.md
@@ -3,9 +3,11 @@ title: dGTPase
layout: article
tableColumns:
article:
- doi: 10.1038/s41564-022-01158-0
+ doi: 10.1038/s41564-022-01158-0
+ abstract: |
+ DNA viruses and retroviruses consume large quantities of deoxynucleotides (dNTPs) when replicating. The human antiviral factor SAMHD1 takes advantage of this vulnerability in the viral lifecycle, and inhibits viral replication by degrading dNTPs into their constituent deoxynucleosides and inorganic phosphate. Here, we report that bacteria use a similar strategy to defend against bacteriophage infection. We identify a family of defensive bacterial deoxycytidine triphosphate (dCTP) deaminase proteins that convert dCTP into deoxyuracil nucleotides in response to phage infection. We also identify a family of phage resistance genes that encode deoxyguanosine triphosphatase (dGTPase) enzymes, which degrade dGTP into phosphate-free deoxyguanosine and are distant homologues of human SAMHD1. Our results suggest that bacterial defensive proteins deplete specific deoxynucleotides (either dCTP or dGTP) from the nucleotide pool during phage infection, thus starving the phage of an essential DNA building block and halting its replication. Our study shows that manipulation of the dNTP pool is a potent antiviral strategy shared by both prokaryotes and eukaryotes.
Sensor: Monitoring of the host cell machinery integrity
- Activator: Direc
+ Activator: Direct
Effector: Nucleotide modifying
PFAM: PF01966, PF13286
contributors:
--
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