Journal
JOURNAL OF PROTEOME RESEARCH
Volume 15, Issue 5, Pages 1388-1401Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.5b00396
Keywords
porcine reproductive and respiratory syndrome virus; nonstructural protein 2; label-free proteomics; proteomics; virus; interactome; aggresomes
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Funding
- Biotechnology and Biological Sciences Research Council [BBS/E/D/20241864] Funding Source: researchfish
- BBSRC [BBS/E/D/20241864] Funding Source: UKRI
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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.
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