Why the study?
Some Type VI CRISPR-Cas systems encode putative membrane proteins that have unclear roles in Cas13-mediated bacterial defense against viruses.
Reveals a novel mechanism where Csx28 acts as a Cas13b-activated effector protein using membrane perturbation for anti-viral defense in bacteria.
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Highlights membrane pores boosting CRISPR defense; leaves open in vivo roles and therapeutic translation.
Type VI CRISPR-Cas systems use the RNA-guided RNase Cas13 to defend bacteria against viruses, and some of these systems encode putative membrane proteins that have unclear roles in Cas13-mediated defense. Here we show that Csx28, of Type VI-B2 systems, forms membrane pore structures to slow cellular metabolism upon viral infection, and this activity drastically increases anti-viral defense. High- resolution cryo-EM reveals that Csx28 exists unexpectedly as a detergent-encapsulated octameric pore, and we then show these Csx28 pores are membrane localized in vivo . Activation of Csx28 in vivo strictly requires sequence-specific recognition of viral mRNAs by Cas13b, and this activation results in Csx28-mediated membrane depolarization, slowed metabolism, and inhibition of sustained viral infection. Together, our work reveals an unprecedented mechanism by which Csx28 acts as a downstream, Cas13b-activated, effector protein that uses membrane perturbation as an anti-viral defense strategy.
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VanderWal et al. (2021) studied this question.
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