ArticleNature communications2025
A toxin-antitoxin system provides phage defense via DNA damage and repair.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Anti-phage defense systems in bacteria: molecular mechanisms and their role in shaping phage therapy strategies.Molecular biology reports · 2026Review
- Structural and functional characterization of VapBC52 toxin-antitoxin system from Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Isolation of novel phages from a resistant Dorea longicatena strain reveals genes associated with phage resistance.Npj viruses · 2026Article
- The molecular mechanisms of the ShosTA system in mediating anti-phage defense.Nucleic acids research · 2026Article
- [Research on Bacteriophage Resistance: Coevolutionary Arms Race Between Bacteria and Phages Drives Novel Antibacterial Therapies].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2026Review
- Bacterial defense systems: Mechanisms, homology to eukaryotic immune systems, and applications.Zoological research · 2026Review
- Hardwired survival algorithms: RelBE1 and MadR1 couple carbon state to metabolic persistence inFrontiers in microbiology · 2026Article
- Prokaryotic homeostasis - a solution to thrive and survive.Frontiers in molecular biosciences · 2025Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Widespread in bacteria and archaea, toxin-antitoxin (TA) systems have been recently demonstrated to function in phage defense. Here we characterize the anti-phage function of a type IV TA system, ShosTA. Using structural and biochemical approaches, we show that ShosT couples phosphoribosyltransferase and pyrophosphatase activities to disrupt purine metabolism, resulting in DNA duplication, cell filamentation and ultimate cell death. ShosA binds DNA and likely recruits other proteins to facilitate DNA homologous recombination to antagonize ShosT's toxicity. We identify Gp0.7 of T7 phage as a trigger for ShosTA system via shutting off the protein synthesis, and the C-terminus-mediated intrinsic instability of ShosA releases the toxicity of the existing ShosT proteins. Collectively, our results provide a novel toxin-antitoxin mechanism for anti-phage immunity and shed light on the triggering of this TA system.
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Registered trials
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