Edinburgh Research Explorer

Characterization of the interactome of the porcine reproductive and respiratory syndrome virus (PRRSV) NSP2 protein reveals the hyper variable region as a binding platform for association with 14-3-3 proteins

Research output: Contribution to journalArticle

Related Edinburgh Organisations

Open Access permissions

Open

Documents

http://pubs.acs.org/doi/10.1021/acs.jproteome.5b00396
Original languageEnglish
Pages (from-to)1388-1401
JournalJournal Of Proteome Research
Volume15
Issue number5
Early online date28 Dec 2015
DOIs
Publication statusPublished - 6 May 2016

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 non-structural 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 non-specific interactions. The interactome data was 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.

Download statistics

No data available

ID: 23064730