Research reveals a novel viral strategy in modulating stress granule formation to promote virus infection PLOSPathogens UBC UCSF virus infection stressgranule viral
By Neha MathurDec 6 2022Reviewed by Danielle Ellis, B.Sc. In a recent study published in PLOS Pathogens, researchers illustrated a novel strategy likely employed by viruses to promote infection.
About the study In one of their previous studies, the researchers observed that CrPV-1A blocked SGs in human cells. In the present study, they set out to determine whether common mechanisms for SG inhibition by CrPV-1A exist in different host species. Study findings The 166 amino acids long CrPV-1A protein modulates SG functions in multiple ways, for instance, by modulating nuclear events, including messenger RNA export and transcription by enrichment of polyadenylation or poly tail in the nucleus. Since mRNAs are a scaffold for SG assembly, the enrichment of poly + tail in the nucleus in CrPV-1A expressing cells might block host mRNA translation and antiviral responses or deplete cytoplasmic mRNA leading to the inhibition of SGs.
Recent studies have shown that Nup358, a unit of the cytoplasmic strand of the nuclear pore complex , localizes to SGs and facilitates the transport of mRNA and protein. In this way, it plays a prominent role in viral infections. Nup358 levels decreased in CrPV-1A-infected cells, and their depletion resulted in SG inhibition.
Immunoblotting for Nup358 in S2 cells showed a protein band at >245 kDa, undetected in Nup358 dsRNA-treated cells, confirming RNAi-mediated depletion of Nup358. The Nup358 depletion had multiple other effects. For instance, pateamine A treatment of Nup358-depleted cells decreased the number of RIN foci per cell.
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