Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein
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Despite a wide presence of type III clustered regularly interspaced short palindromic repeats, CRISPR-associated (CRISPR-Cas) in archaea and bacteria, very few anti-CRISPR (Acr) proteins inhibiting type III immunity have been identified, and even less is known about their inhibition mechanism. Here, we present the discovery of a type III CRISPR-Cas inhibitor, AcrIIIB2, encoded by Sulfolobus virus S. islandicus rod-shaped virus 3 (SIRV3). AcrIIIB2 inhibits type III-B CRISPR-Cas immune response to protospacers encoded in middle/late-expressed viral genes. Investigation of the interactions between S. islandicus type III-B CRISPR-Cas Cmr-α-related proteins and AcrIIIB2 reveals that the Acr does not bind to Csx1 but rather interacts with the Cmr-α effector complex. Furthermore, in vitro assays demonstrate that AcrIIIB2 can block the dissociation of cleaved target RNA from the Cmr-α complex, thereby inhibiting the Cmr-α turnover, thus preventing host cellular dormancy and further viral genome degradation by the type III-B CRISPR-Cas immunity.
Originalsprog | Engelsk |
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Tidsskrift | Cell Host and Microbe |
Vol/bind | 31 |
Udgave nummer | 11 |
Sider (fra-til) | 1837-1849.e5 |
Antal sider | 19 |
ISSN | 1931-3128 |
DOI | |
Status | Udgivet - 2023 |
Bibliografisk note
Funding Information:
This work was supported by the Danish Council for Independent Research/Natural Sciences (DFF-0135-00402) and Novo Nordisk Foundation/Hallas Moeller Ascending Investigator Grant (NNF17OC0031154) to X.P. X.P. conceived the project. J.L. L.A. and Y.B.-C. designed experiments. J.L. and L.A. performed experiments. J.L. L.A. Y.B.-C. and X.P. analyzed the data. J.L. made the figures. J.L. and L.A. wrote the draft. All authors revised the manuscript. The authors declare no competing interests. We support inclusive, diverse, and equitable conduct of research.
Publisher Copyright:
© 2023 Elsevier Inc.
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