The glycoprotein 5(GP5) of porcine reproductive and respiratory syndrome virus(PRRSV) is a multi-functional protein that plays important roles in virus assembly,entry and viral anti-host responses.In the present study,we investigated the cellular binding partners of GP5 by using lentivirus transduction coupled with immunoprecipitation and mass spectrometry.There were about 40 cellular proteins identified with high Confidence Icons by MS/MS.Ingenuity Pathway Analysis(IPA)indicated that these proteins could be assigned to different functional classes and networks.Furthermore,we validated some of the interactions by co-immunoprecipitation(Co-IP) and confocal microscopy,including those with mitofilin,a mitochondrial inner membrane protein that might be involved in PRRSV or GP5-induced apoptosis,and calnexin,a protein chaperone that might facilitate the folding and maturation of GP5.The interactome data contribute to understand the role and molecular mechanisms of GP5 in PRRSV pathogenesis.
supported by the Earmarked Fund for Modern Agro-industry Technology Research System of China (CARS-36) from the Ministry of Agriculture of China;the National Natural Science Foundation of China (31572549);the National Key Technology R&D Program of China (2015BAD12B01-2) from the Ministry of Science and Technology of China