Mass Spectrometry-Based Proteomic Analysis of Porcine Reproductive and Respiratory Syndrome Virus NSP9 Protein with Host Proteins.

ABSTRACT: Porcine reproductive and respiratory syndrome virus (PRRSV) nonstructural protein 9 (NSP9), the viral RNA-dependent RNA polymerase (RdRp), is essential for viral replication but its comprehensive host interactome remains uncharacterized. This study employed co-immunoprecipitation coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) to systematically identify NSP9-associated host proteins. We identified 222 high-confidence host interactors, with Gene Ontology and KEGG pathway analyses revealing significant enrichment in RNA/DNA-binding proteins, ubiquitin-proteasome pathways, metabolic regulators (amino acid/lipid biosynthesis), endoplasmic reticulum processing, and cell cycle components. Protein-protein interaction network analysis further delineated six functional module

SUBMITTER: Wen W 

PROVIDER: S-EPMC12730103 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature