Systematic Analysis of Lysine Succinylation in Vero cells infected with Small Ruminant Morbillivirus

Small ruminant morbillivirus (SRMV), formerly named Peste-des-petits ruminants virus (PPRV), belongs to the genus Morbillivirus in the family Paramyxoviridae and causes a highly contagious disease in small ruminants, especially goats and sheep. Lysine succinylation is a newly identified and conserved modification and plays an important role in host cell response to pathogen infection. Here, we present a global analysis of the succinylome of SRMV-infected Vero cell using succinylation specific antibody-based enrichment and dimethylation labeling-based quantitative proteomics. As a result, 2633 succinylation sites derived from 823 cellular proteins were quantified. Comparative analysis revealed that 228 down-regulated succinylation sites on 139 proteins and 44 up-regulated succinylation sites on 38 proteins were significantly modified in response to SRMV infection, seven lysine succinylation motifs were identified. Bioinformatics analysis showed that the succinylated proteins mainly participated in cellular respiration and biosynthetic process. Protein-protein interaction networks of the identified proteins provided further evidence that a variety of ATP synthase subunits and carbon metabolism were modulated by succinylation while the overlapped proteins between succinylation and acetylation are involved in glyoxylate and dicarboxylate metabolism. Taken together, these findings provide the first report of succinylome in SRMV infection, lysine acetylation may have a more important effect than succinylation in SRMV infection. These findings provide a novel view on investigating the pathogenic mechanism of SRMV.