PMC:7640975 / 47027-48606 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7640975","sourcedb":"PMC","sourceid":"7640975","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7640975","text":"The interactions between host cells and viruses are highly complex, which usually involves numerous alterations in the expression of diverse genes, mRNAs, and proteins.36,37 Deciphering the laws behind these changes over the course of viral infection plays a vital role in elucidating the pathogenic mechanisms and in developing efficacious antiviral strategies.37 Over the past decade, MS-based proteomic techniques have contributed significantly to uncovering more factors and mechanisms related to viral infections and the corresponding host cellular pathophysiological processes.18 However, no research to date has focused on differential proteomic analysis of global protein profiles in host cells upon infection by PDCoV. In this study, iTRAQ combined with LC-MS/MS was used to identify the DEPs in PDCoV-infected IPEC-J2 cells. Although various cell lines including ST, LLC-PK1, PK-15, and IPI-2I cells have been shown to be highly permissive to PDCoV infection,17,34,38 considering porcine enterocytes are the natural targets for PDCoV infection in vivo,8,9 we chose to use IPEC-J2 cells for the proteomic analysis with the goal of obtaining experimental data that could better reflect the physiological state of pigs and the true state of PDCoV infection in vivo. Ultimately, a total of 78 DEPs were identified in PDCoV-infected IPEC-J2 cells, among which 23 proteins were significantly upregulated and 55 proteins were significantly downregulated. Moreover, we also identified six viral proteins including the spike, membrane, nucleocapsid, NS6, NS7, and Nsp5 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