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TitleCsx28 is a membrane pore that enhances CRISPR-Cas13b-dependent antiphage defense.
Journal, issue, pagesScience, Vol. 380, Issue 6643, Page 410-415, Year 2023
Publish dateApr 28, 2023
AuthorsArica R VanderWal / Jung-Un Park / Bogdan Polevoda / Julia K Nicosia / Adrian M Molina Vargas / Elizabeth H Kellogg / Mitchell R O'Connell /
PubMed AbstractType 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- ...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.
External linksScience / PubMed:37104586 / PubMed Central
MethodsEM (single particle)
Resolution3.65 Å
Structure data

40059

8gi1

EMDB-40059, PDB-8gi1:
Homo-octamer of PbuCsx28 protein
Method: EM (single particle) / Resolution: 3.65 Å

Source
  • prevotella buccae (bacteria)
KeywordsANTIVIRAL PROTEIN / CRISPR-associated protein

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