ArticleNature communications2025
Phages carry orphan antitoxin-like enzymes to neutralize the DarTG1 toxin-antitoxin defense system.
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 10 papers.
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Who cites it
10 citing papers in PubMed.
- How bacterial immune systems sense phage infection.Nature reviews. Microbiology · 2026Review
- Article
- Systematic mapping of bacteriophage gene essentiality with HIDEN-SEQ.Nature microbiology · 2026Article
- Phage-encoded NARP3 system rebuilds NADScience advances · 2026Article
- Phage host range: determinants, dynamics and applications.Nature reviews. Microbiology · 2026Review
- Linear-time prediction of proteome-scale microbial protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Expanding Landscape of ADP-Ribosylation: Protein, DNA, RNA, and Mitochondrial Regulation.Chemical research in toxicology · 2026Review
- The phage nucleus synergizes with an anti-defense protein to resist bacterial immunity.Cell reports · 2026Article
- ADP-Ribosylation of Cytidine: A Novel Nucleic Acid Modification Reversed by NADAR Hydrolases.Toxins · 2026Article
- Beyond plasmid addiction: the role of toxin-antitoxin systems in the selfish behavior of mobile genetic elements.Journal of bacteriology · 2025Review
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Abstract
The astounding number of anti-phage defenses encoded by bacteria is countered by an elaborate set of phage counter-defenses, though their evolutionary origins are often unknown. Here, we report the discovery of an orphan antitoxin counter-defense element in T4-like phages that can overcome the bacterial toxin-antitoxin phage defense system, DarTG1. The DarT1 toxin, an ADP-ribosyltransferase, modifies phage DNA to prevent replication while its cognate antitoxin, DarG1, is a NADAR superfamily ADP-ribosylglycohydrolase that reverses these modifications in uninfected bacteria. We show that some phages carry an orphan DarG1-like NADAR domain protein, which we term anti-DarT factor NADAR (AdfN), that removes ADP-ribose modifications from phage DNA during infection thereby enabling replication in DarTG1-containing bacteria. We find divergent NADAR proteins in unrelated phages that likewise exhibit anti-DarTG1 activity, underscoring the importance of ADP-ribosylation in bacterial-phage interactions, and revealing the function of a substantial subset of the NADAR superfamily.
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