ArticleNature structural & molecular biology2019
An anti-CRISPR protein disables type V Cas12a by acetylation.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
74 citing papers in PubMed.
- Article
- Revisiting the life cycle of temperate phages.Nature reviews. Microbiology · 2026Review
- Phage tail protein methylation enabling the virus to bind to the surface of bacterial cells is vital for progeny infectivity.Cell insight · 2026Article
- Beyond DNA editing: how Cas13 redefined programmable RNA manipulation and what still limits its therapeutic promise.Nucleic acids research · 2026Review
- Review
- Simultaneous inhibition of bacterial virulence and anti-phage defense systems by synergistic bacteriophage counter-defense proteins.The EMBO journal · 2026Article
- An anti-CRISPR targets the sgRNA to block Cas9 and guides the design of enhanced genome editors.Nature structural & molecular biology · 2026Article
- Multilayer regulation of CRISPR systems: integrating anti-CRISPR proteins, CRISPRi/a, and quorum sensing networks.Frontiers in cellular and infection microbiology · 2026Review
- Colocalisation of lanthipeptide production with genetic exchange and defence systems across prokaryote genomes.BMC genomics · 2025Article
- Article
- Rational engineering of allosteric protein switches by in silico prediction of domain insertion sites.Nature methods · 2025Article
- Engineering stimuli-responsive CRISPR-Cas systems for versatile biosensing.Analytical and bioanalytical chemistry · 2025Review
- Proteomic Analysis of Marine Bacteriophages: Structural Conservation, Post-Translational Modifications, and Phage-Host Interactions.Environmental microbiology · 2025Article
- Phages carry orphan antitoxin-like enzymes to neutralize the DarTG1 toxin-antitoxin defense system.Nature communications · 2025Article
- Versatile plant genome engineering using anti-CRISPR-Cas12a systems.Science China. Life sciences · 2024Article
- Diverse viral cas genes antagonize CRISPR immunity.Nature · 2024Article
- Phages carry orphan antitoxin-like enzymes to neutralize the DarTG1 toxin-antitoxin defense system.bioRxiv : the preprint server for biology · 2024Article
- Increasing CRISPR/Cas9-mediated gene editing efficiency in T7 phage by reducing the escape rate based on insight into the survival mechanism.Acta biochimica et biophysica Sinica · 2024Article
- CRISPR/Cpf1-FOKI-induced gene editing inSynthetic and systems biotechnology · 2024Article
- Insights into the inhibition of protospacer integration via direct interaction between Cas2 and AcrVA5.Nature communications · 2024Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phages use anti-CRISPR proteins to deactivate the CRISPR-Cas system. The mechanisms for the inhibition of type I and type II systems by anti-CRISPRs have been elucidated. However, it has remained unknown how the type V CRISPR-Cas12a (Cpf1) system is inhibited by anti-CRISPRs. Here we identify the anti-CRISPR protein AcrVA5 and report the mechanisms by which it inhibits CRISPR-Cas12a. Our structural and biochemical data show that AcrVA5 functions as an acetyltransferase to modify Moraxella bovoculi (Mb) Cas12a at Lys635, a residue that is required for recognition of the protospacer-adjacent motif. The AcrVA5-mediated modification of MbCas12a results in complete loss of double-stranded DNA (dsDNA)-cleavage activity. In contrast, the Lys635Arg mutation renders MbCas12a completely insensitive to inhibition by AcrVA5. A cryo-EM structure of the AcrVA5-acetylated MbCas12a reveals that Lys635 acetylation provides sufficient steric hindrance to prevent dsDNA substrates from binding to the Cas protein. Our study reveals an unprecedented mechanism of CRISPR-Cas inhibition and suggests an evolutionary arms race between phages and bacteria.
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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.