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TitleAcrVIB1 inhibits CRISPR-Cas13b immunity by promoting unproductive crRNA binding accessible to RNase attack.
Journal, issue, pagesMol Cell, Vol. 85, Issue 6, Page 1162-11175.e7, Year 2025
Publish dateMar 20, 2025
AuthorsKatharina G Wandera / Stefan Schmelz / Angela Migur / Anuja Kibe / Peer Lukat / Tatjana Achmedov / Neva Caliskan / Wulf Blankenfeldt / Chase L Beisel /
PubMed AbstractAnti-CRISPR proteins (Acrs) inhibit CRISPR-Cas immune defenses, with almost all known Acrs acting on the Cas nuclease-CRISPR (cr)RNA ribonucleoprotein (RNP) complex. Here, we show that AcrVIB1 from ...Anti-CRISPR proteins (Acrs) inhibit CRISPR-Cas immune defenses, with almost all known Acrs acting on the Cas nuclease-CRISPR (cr)RNA ribonucleoprotein (RNP) complex. Here, we show that AcrVIB1 from Riemerella anatipestifer, the only known Acr against Cas13b, principally acts upstream of RNP complex formation by promoting unproductive crRNA binding followed by crRNA degradation. AcrVIB1 tightly binds to Cas13b but not to the Cas13b-crRNA complex, resulting in enhanced rather than blocked crRNA binding. However, the more tightly bound crRNA does not undergo processing and fails to activate collateral RNA cleavage even with target RNA. The bound crRNA is also accessible to RNases, leading to crRNA turnover in vivo even in the presence of Cas13b. Finally, cryoelectron microscopy (cryo-EM) structures reveal that AcrVIB1 binds a helical domain of Cas13b responsible for securing the crRNA, keeping the domain untethered. These findings reveal an Acr that converts an effector nuclease into a crRNA sink to suppress CRISPR-Cas defense.
External linksMol Cell / PubMed:39965569
MethodsEM (single particle)
Resolution3.09 - 5.11 Å
Structure data

50322

9fcv

EMDB-50322, PDB-9fcv:
Cas nuclease-CRISPR (cr)RNA ribonucleoprotein (RNP) complex
Method: EM (single particle) / Resolution: 3.09 Å

EMDB-51509: PbuCas13b-crRNA complex, open conformation
Method: EM (single particle) / Resolution: 4.23 Å

EMDB-51513: PbuCas13b Helical-2 domain in complex with anti-CRISPR protein (AcrVIB1)
Method: EM (single particle) / Resolution: 5.11 Å

Source
  • segatella buccae (bacteria)
  • synthetic construct (others)
  • Riemerella anatipestifer (bacteria)
KeywordsRNA BINDING PROTEIN / AcrVIB1; anti-CRISPR protein; Cas13b

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