Viral condensates formed by Pea enation mosaic virus 2 sequester ribosomal components and suppress translation.

ABSTRACT: Viral proteins with intrinsic disorder, such as the p26 movement protein from Pea enation mosaic virus 2 (PEMV2), can phase separate and form condensates that aid specific stages of virus replication. However, little is known about the impact of viral condensate formation on essential cellular processes, like translation. In this study, we performed mass spectrometry on affinity-purified p26 condensates and found an enrichment of RNA-binding proteins involved in translation and ribosome biogenesis. Puromycin assays and polysome profiling show that ectopic p26 expression suppresses ribosome assembly and translation in Nicotiana benthamiana, mirroring defects in late-stage PEMV2 infection. Despite interactions with the 2'-O-methyltransferase fibrillarin, p26 does not inhibit translation by a

SUBMITTER: Brown SL 

PROVIDER: S-EPMC11649027 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature