Abstract
Background: Bovine parainfluenza virus type 3 (BPIV3) infection often causes respiratory tissue damage and immunosuppression and results in bovine respiratory disease complex. Bovine respiratory disease complex is one of the major diseases in dairy cattle and causes huge economical losses every year. The pathogenetic and immunoregulatory mechanisms involved in the process of BPIV3 infection, however, remain unknown. Proteomics is a powerful tool for high-throughput identification of proteins and has been widely used to understand how viruses interact with host cells.Methods: In the present study, we report a proteomic analysis to investigate the whole cellular protein alterations of MDBK cells infected with BPIV3. To investigate the infection process of BPIV3 and the immune response mechanism of MDBK cells, isobaric tags for relative and absolute quantitation analysis (iTRAQ) and Q-Exactive mass spectrometry-based proteomics were performed. The differentially expressed proteins (DEPs) involved in the BPIV3 invasion process in MDBK cells were identified, annotated, and quantitated.Results: A total of 116 proteins, which included 74 upregulated proteins and 42 downregulated proteins, were identified as DEPs between the BPIV3-infected and the mock-infected groups. These DEPs included corresponding proteins related to inflammatory response, immune response, and lipid metabolism. These results might provide some insights for understanding the pathogenesis of BPIV3. Fluorescent quantitative PCR and western blotting analysis showed results consistent with those of iTRAQ identification. Interestingly, the upregulated protein MKK3 was associated with the p38 MAPK signaling pathway.Conclusions: The results of proteomics analysis indicated BPIV3 infection could activate the p38 MAPKpathway to promote virus replication.
Antigenic Analysis of Human and Bovine Parainfluenza Virus Type 3 Strains with Monoclonal Antibodies
