The full-length nsp2 replicase contributes to viral assembly in highly pathogenic PRRSV-2.

ABSTRACT: Porcine reproductive and respiratory syndrome viruses (PRRSVs) are significant pathogens that affect the global swine industry. Its virions consist of a central core composed of nucleocapsid (N) protein, surrounded by multiple distinct viral envelope proteins. However, the mechanisms underlying the recognition and packaging of N protein by viral envelope proteins remain elusive. In this study, we elucidated the role of nonstructural protein 2 (nsp2) from highly pathogenic PRRSV-2 (HP-PRRSV-2) in viral assembly. Firstly, among all the tested envelope proteins, only glycoprotein 5 (GP5) exhibits limited interaction with N protein. Interestingly, we demonstrated that full-length nsp2 co-immunoprecipitates (Co-IPs) with the N protein and all tested viral envelope proteins. In the presence of f

SUBMITTER: Bai Y-Z 

PROVIDER: S-EPMC11784222 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature