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Anti-CRISPR proteins encoded by archaeal lytic viruses inhibit subtype I-D immunity
Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
Dokumenter
- Anti-CRISPR
Accepteret manuskript, 19,5 MB, PDF-dokument
DOI
- https://doi.org/10.1038/s41564-018-0120-z
Forlagets udgivne version
- Fei He, Københavns Universitet ,
- Yuvaraj Bhoobalan-Chitty, Københavns Universitet ,
- Lan B Van
- Anders L Kjeldsen, Københavns Universitet ,
- Matteo Dedola, Københavns Universitet ,
- Kira S Makarova, National Center for Biotechnology Information, National Library of Medicine, NIH, Bethesda, USA ,
- Eugene V Koonin, National Center for Biotechnology Information, National Library of Medicine, NIH, Bethesda, USA ,
- Ditlev E Brodersen
- Xu Peng, Københavns Universitet
Viruses employ a range of strategies to counteract the prokaryotic adaptive immune system, clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins (CRISPR-Cas), including mutational escape and physical blocking of enzymatic function using anti-CRISPR proteins (Acrs). Acrs have been found in many bacteriophages but so far not in archaeal viruses, despite the near ubiquity of CRISPR-Cas systems in archaea. Here, we report the functional and structural characterization of two archaeal Acrs from the lytic rudiviruses, SIRV2 and SIRV3. We show that a 4 kb deletion in the SIRV2 genome dramatically reduces infectivity in Sulfolobus islandicus LAL14/1 that carries functional CRISPR-Cas subtypes I-A, I-D and III-B. Subsequent insertion of a single gene from SIRV3, gp02 (AcrID1), which is conserved in the deleted fragment, successfully restored infectivity. We demonstrate that AcrID1 protein inhibits the CRISPR-Cas subtype I-D system by interacting directly with Cas10d protein, which is required for the interference stage. Sequence and structural analysis of AcrID1 show that it belongs to a conserved family of compact, dimeric αβ-sandwich proteins characterized by extreme pH and temperature stability and a tendency to form protein fibres. We identify about 50 homologues of AcrID1 in four archaeal viral families demonstrating the broad distribution of this group of anti-CRISPR proteins.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Nature Microbiology |
| Vol/bind | 3 |
| Nummer | 4 |
| Sider (fra-til) | 461-469 |
| Antal sider | 9 |
| DOI | |
| Status | Udgivet - apr. 2018 |
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