期刊
CELL
卷 179, 期 2, 页码 448-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2019.09.003
关键词
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资金
- Danish Council for Independent Research/Technology and Production [DFF-7017-00060]
- Novo Nordisk Fonden/Hallas MOller Ascending Investigator Grant [NNF17OC0031154]
- Novo Nordisk Foundation Laureate Research Grant
Bacteria and archaea possess a striking diversity of CRISPR-Cas systems divided into six types, posing a significant barrier to viral infection. As part of the virus-host arms race, viruses encode protein inhibitors of type I, II, and V CRISPR-Cas systems, but whether there are natural inhibitors of the other, mechanistically distinct CRI - R-Cas types is unknown. Here, we present the discovery of a type III CRISPR-Cas inhibitor, AcrIIIB1, encoded by the Sulfolobus virus SIRV2. AcrIIIB1 exclusively inhibits CRISPR-Cas subtype III-B immunity mediated by the RNase activity of the accessory protein Csx1. AcrIIIB1 does not appear to bind Csx1 but, rather, interacts with two distinct subtype III-B effector complexes-Cmr-alpha and Cmr-gamma-which, in response to protospacer transcript binding, are known to synthesize cyclic oligoadenylates (cOAs) that activate the Csx1 collateral RNase. Taken together, we infer that AcrIIIB1 inhibits type HI-B CRISPR-Cas immunity by interfering with a Csx1 RNase-related process.
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