Background: Peste des petits ruminants virus (PPRV) is a negative-stranded RNA virus belonging to the Paramyxoviridae family and causes acute, highly contagious disease in small ruminants. Lysine acetylation plays central role in regulating gene expression. However, the extent and function of lysine acetylation in host cells during PPRV infection remains unknown. Methods: Lysine acetylation of PPRV-infected Vero cells was tested and differentially expressed lysine acetylation was found. The acetylated peptides were enriched using specific antibody and labeled with demethylation. Proteins with acetylation sites were identified. Subsequently, intensive bioinformatics analysis of succinylome of PPRV-infected Vero cells was were performed. In this study, intensive proteomic quantification analysis of the proteome and acetylome of PPRV-infected Vero cells was performed using dimethylation labeling-based quantitative proteomics. Results: We identified 4729 cellular proteins and 1068 proteins with 2641 modification sites quantifiable detected by mass spectrometry, of which 304 proteins with 410 acetylation sites were significantly acetylated in response to PPRV infection. Bioinformatics analyses revealed that the differentially acetylated proteins mainly participated in carbohydrate catabolic and DNA metabolic process, and were associated with multifarious functions, suggesting that intracellular activities were extensively changed after PPRV infection. Protein-protein interaction (PPI) network of the identified proteins further indicated that a variety of chaperone and ribosome processes were modulated by acetylation. Conclusions: To our knowledge, this is the first study on acetylome in host cell infected with PPRV. It provides an important baseline to future study the roles of acetylation in the host response to PPRV replication.
