Phosphorylation tunes strain-specific protein condensation during rotavirus replication organelle assembly

ABSTRACT: In many viruses, intrinsically disordered proteins (IDPs) drive the formation of replicative organelles via liquid-liquid phase separation (LLPS). In species A rotaviruses, the disordered protein NSP5 forms condensates with NSP2, but its high sequence diversity raises questions about whether this mechanism is conserved across strains. Using a machine learning approach, we show that NSP5 variants differ significantly in LLPS propensity. We engineered an NSP5 variant with features derived from strains with low LLPS propensity (low-LLPS). Despite lacking the ability to phase separate in vitro unless phosphorylated, this variant nevertheless supported condensate formation and viral replication in cells. We found that low-LLPS variants require phosphorylation to nucleate phase separation, where

SUBMITTER: Julia Acker 

PROVIDER: S-SCDT-10_1038-S44318-026-00814-Z | biostudies-other |

REPOSITORIES: biostudies-other