Proteomic profiling of pseudorabies virus-infected PK-15 cells based on 4D label free analysis.

Pseudorabies virus (PRV) heavily depends on host machinery to support its life cycle. Investigating the interaction between PRV and host could aid in the understandings of viral pathogenesis. In this study, we performed a 4D label free proteomic method to examine the differentially expressed proteins in porcine kidney PK-15 cells with PRV infection. The results showed that the levels of 661 proteins were significantly elevated and 693 proteins were markedly reduced. Furthermore, these altered proteins were primarily enriched in spliceosome, protein processing in endoplasmic reticulum (ER), RNA transport, and protein export. To ensure the reliability of the proteomic results, the protein levels of formin binding protein 11 and wolfram syndrome 1as components of spliceosome and ER were verified via western blotting and the results were consistent. Together, our data shed light on a new protein profiling induced by PRV infection and highlighted the importance of spliceosome and ER in PRV replication which could promote understandings of host-PRV interplay.