Journal
SCIENCE
Volume 380, Issue 6643, Pages 410-415Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abm1184
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In this study, researchers discovered that the membrane protein Csx28 in Type VI CRISPR-Cas systems enhances antiviral defense by slowing cellular metabolism upon viral infection. The antiviral activity of Csx28 requires sequence-specific cleavage of viral messenger RNAs by Cas13b. High-resolution cryo-electron microscopy revealed that Csx28 forms an octameric pore-like structure, which localizes to the inner membrane in vivo.
Type VI CRISPR-Cas systems use RNA-guided ribonuclease (RNase) Cas13 to defend bacteria against viruses, and some of these systems encode putative membrane proteins that have unclear roles in Cas13-mediated defense. We show that Csx28, of type VI-B2 systems, is a transmembrane protein that assists to slow cellular metabolism upon viral infection, increasing antiviral defense. High-resolution cryo-electron microscopy reveals that Csx28 forms an octameric pore-like structure. These Csx28 pores localize to the inner membrane in vivo. Csx28's antiviral activity in vivo requires sequence-specific cleavage of viral messenger RNAs by Cas13b, which subsequently results in membrane depolarization, slowed metabolism, and inhibition of sustained viral infection. Our work suggests a mechanism by which Csx28 acts as a downstream, Cas13b-dependent effector protein that uses membrane perturbation as an antiviral defense strategy.
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