ArticleNature microbiology2024
Reversible conjugation of a CBASS nucleotide cyclase regulates bacterial immune response to phage infection.
Article in Nature microbiology, 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, 20 citations in OpenAlex.
- Inhibition by ATP regulates the activity of a CBASS anti-phage nucleotide cyclase.The Biochemical journal · 2026Article
- Article
- Mechanistic basis for protein conjugation in a diverged bacterial ubiquitination pathway.Nature structural & molecular biology · 2026Article
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- Article
- Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity.Science (New York, N.Y.) · 2025Article
- Abundant bacterial nucleoid-associated protein H-NS limits plasmid transfer through mechanical modification of DNA.Nucleic acids research · 2025Article
- Lactococcal mobile genetic elements harbour a diverse phage defensome rich in restriction-modification systems.Nucleic acids research · 2025Article
- Diversity and abundance of ring nucleases in type III CRISPR-Cas loci.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Heterologous expression of the M. abscessus CBASS system confers phage TM4 resistance in M. smegmatis.BMC microbiology · 2025Article
- The evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.Current opinion in structural biology · 2025Review
- Sequestering survival: sponge-like proteins in phage evasion of bacterial immune defenses.Frontiers in immunology · 2025Review
- Nucleotide Immune Signaling in CBASS, Pycsar, Thoeris, and CRISPR Antiphage Defense.Annual review of microbiology · 2024Review
- A large-scale type I CBASS antiphage screen identifies the phage prohead protease as a key determinant of immune activation and evasion.Cell host & microbe · 2024Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Prokaryotic antiviral defence systems are frequently toxic for host cells and stringent regulation is required to ensure survival and fitness. These systems must be readily available in case of infection but tightly controlled to prevent activation of an unnecessary cellular response. Here we investigate how the bacterial cyclic oligonucleotide-based antiphage signalling system (CBASS) uses its intrinsic protein modification system to regulate the nucleotide cyclase. By integrating a type II CBASS system from Bacillus cereus into the model organism Bacillus subtilis, we show that the protein-conjugating Cap2 (CBASS associated protein 2) enzyme links the cyclase exclusively to the conserved phage shock protein A (PspA) in the absence of phage. The cyclase-PspA conjugation is reversed by the deconjugating isopeptidase Cap3 (CBASS associated protein 3). We propose a model in which the cyclase is held in an inactive state by conjugation to PspA in the absence of phage, with conjugation released upon infection, priming the cyclase for 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.