Plant negative-strand RNA virus phosphoprotein condensates exploit host trafficking and lipid synthesis for viral factory assembly.

ABSTRACT: RNA viruses often remodel host intracellular membranes to establish specialized replication compartments through viral protein-induced phase separation. However, the mechanisms underlying membrane remodeling and the characteristics that render these sites conducive to replication remain poorly understood, particularly in plant negative-strand RNA viruses. Here, we demonstrate that the phosphoprotein (P) of rice stripe mosaic virus (RSMV) forms biomolecular condensates via liquid-liquid phase separation (LLPS) to recruit essential components for viral replication factories (VFs). We identify a direct interaction between RSMV P and adenosine diphosphate (ADP) ribosylation factor 1 (OsARF1C), a crucial regulator of the coatomer protein I (COP I) vesicle transport pathway that is vital for vir

SUBMITTER: Wang Z 

PROVIDER: S-EPMC12366689 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature