ArticleCell host & microbe2024
A large-scale type I CBASS antiphage screen identifies the phage prohead protease as a key determinant of immune activation and evasion.
Article in Cell host & microbe, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- How bacterial immune systems sense phage infection.Nature reviews. Microbiology · 2026Review
- CBASS limits bacteriophage production while maintaining cell viability in Pseudomonas aeruginosa.Cell host & microbe · 2026Article
- Inhibition by ATP regulates the activity of a CBASS anti-phage nucleotide cyclase.The Biochemical journal · 2026Article
- Review
- A bacterial CARD-NLR-like immune system controls the release of gene transfer agents.Nature microbiology · 2026Article
- Discovery of Small-Molecule Inhibitors of the Pycsar Antiphage Defense.ACS chemical biology · 2026Article
- Nuclease-NTPase antiphage defence systems use conserved molecular features to control bacterial immunity.Nature microbiology · 2026Article
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- Viral effectors trigger innate immunity across the tree of life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- A widespread family of viral sponge proteins reveals specific inhibition of nucleotide signals in anti-phage defense.Molecular cell · 2025Article
- Heterologous expression of the M. abscessus CBASS system confers phage TM4 resistance in M. smegmatis.BMC microbiology · 2025Article
- An archaeal chronic virus escapes the immunity of prokaryotic Argonaute.Nucleic acids research · 2025Article
- Article
- Review
- Discovery of antiphage systems in the lactococcal plasmidome.Nucleic acids research · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Cyclic oligonucleotide-based signaling system (CBASS) is an antiviral system that protects bacteria from phage infection and is evolutionarily related to human cGAS-STING immunity. cGAS-STING signaling is initiated by the recognition of viral DNA, but the molecular cues activating CBASS are incompletely understood. Using a screen of 975 type I CBASS operon-phage challenges, we show that operons with distinct cGAS/DncV-like nucleotidyltransferases (CD-NTases) and CD-NTase-associated protein (Cap) effectors exhibit marked patterns of phage restriction. We find that some type I CD-NTase enzymes require a C-terminal AGS-C immunoglobulin (Ig)-like fold domain for defense against select phages. Escaper phages evade CBASS via protein-coding mutations in virion assembly proteins, and acquired resistance is largely operon specific. We demonstrate that the phage Bas13 prohead protease interacts with the CD-NTase EcCdnD12 and can induce CBASS-dependent growth arrest in cells. Our results define phage virion assembly as a determinant of type I CBASS immune evasion and support viral protein recognition as a putative mechanism of cGAS-like enzyme activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.