ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.

ABSTRACT: Nucleoproteins (N) of negative-sense RNA viruses exhibit an inherent tendency to oligomerize, forming a ribonucleoprotein complex that protects the viral genome. Here, immunoprecipitation coupled with mass spectrometry is used to identify zinc ribbon domain containing 2 (ZNRD2) as a host interactor for the respiratory syncytial virus (RSV) N protein. The results demonstrated that ZNRD2 functions as a restriction factor against RSV by enhancing the oligomerization and insolubility of N. Conversely, RSV N sequesters ZNRD2 into an insoluble aggregate, rendering it incapable of performing physiological functions required for the quality control of chaperonin assembly. Notably, RSV phosphoprotein (P) completely inhibited the formation of the insoluble ZNRD2-RSV N complex by maintaining N in a m

SUBMITTER: Zhou H 

PROVIDER: S-EPMC12948206 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature