Characterization of the Interactome of the Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 2 Reveals the Hyper Variable Region as a Binding Platform for Association with 14-3-3 Proteins


Xiao, Yihong, Wu, Weining, Gao, Jiming, Smith, Nikki, Burkard, Christine, Xia, Dong, Zhang, Minxia, Wane, Chengbao, Archibald, Alan, Digard, Paul et al (show 2 more authors) (2016) Characterization of the Interactome of the Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 2 Reveals the Hyper Variable Region as a Binding Platform for Association with 14-3-3 Proteins. JOURNAL OF PROTEOME RESEARCH, 15 (5). pp. 1388-1401.

[img] Text
With track changes.DOCX - Author Accepted Manuscript
Download (88kB)

Abstract

Porcine reproductive and respiratory syndrome virus (PRRSV) is a major threat to the swine industry worldwide and hence global food security, exacerbated by a newly emerged highly pathogenic (HP-PRRSV) strain from China. PRRSV nonstructural protein 2 (nsp2) is a multifunctional polypeptide with strain-dependent influences on pathogenicity. A number of discrete functional regions have been identified on the protein. Quantitative label free proteomics was used to identify cellular binding partners of nsp2 expressed by HP-PRRSV. This allowed the identification of potential cellular interacting partners and the discrimination of nonspecific interactions. The interactome data were further investigated and validated using biological replicates and also compared with nsp2 from a low pathogenic (LP) strain of PRRSV. Validation included both forward and reverse pulldowns and confocal microscopy. The data indicated that nsp2 interacted with a number of cellular proteins including 14-3-3, CD2AP, and other components of cellular aggresomes. The hyper-variable region of nsp2 protein was identified as a binding platform for association with 14-3-3 proteins.

Item Type: Article
Uncontrolled Keywords: porcine reproductive and respiratory syndrome virus, nonstructural protein 2, label-free proteomics, proteomics, virus, interactome, aggresomes
Depositing User: Symplectic Admin
Date Deposited: 28 Oct 2016 08:54
Last Modified: 19 Jan 2023 07:27
DOI: 10.1021/acs.jproteome.5b00396
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3004175
Dimensions
Altmetric
CORE (COnnecting REpositories)