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Comprehensive analysis of the succinylome in Vero cells infected with peste des petits ruminants virus Nigeria 75/1 vaccine strain

文献类型： 外文期刊

作者： Meng, Xuelian 1 ; Zhu, Xueliang 1 ; Wang, Xiangwei 1 ; Zhang, Rui 2 ; Zhang, Zhidong 2 ; Sun, Yuefeng 1 ;

作者机构： 1.Chinese Acad Agr Sci, State Key Lab Anim Dis Control & Prevent, Lanzhou Vet Res Inst, Xujiaping 1, Lanzhou 730046, Gansu, Peoples R China

2.Southwest Minzu Univ, Coll Anim & Vet Sci, 16 South Sect,1st Ring Rd, Chengdu 610041, Sichuan, Peoples R China

关键词： Post-translational modification; Succinylation; Protein-protein interaction; Peste Des petits ruminants virus

期刊名称：BMC VETERINARY RESEARCH （ 影响因子：2.6； 五年影响因子：2.7 ）

ISSN：

年卷期： 2025 年 21 卷 1 期

页码：

收录情况： SCI

摘要： BackgroundPeste des petits ruminants virus (PPRV) is currently the only member of the Morbillivirus caprinae species within the genus Morbillivirus of the family Paramyoxviridae. PPRV causes a highly contagious disease in small ruminants, especially goats and sheep. Succinylation is a newly identified and conserved modification and plays an important role in host cell response to pathogen infection. However, the extent and function of succinylation in Vero cells during PPRV infection remains unknown.ResultsIn this study, a global profile of the succinylome in Vero cells infected with PPRV Nigeria 75/1 vaccine strain (PPRVvac) was performed by dimethylation labeling-based quantitative proteomics analysis. A total of 2633 succinylation sites derived from 823 proteins were quantified. The comparative analysis of differentially succinylated sites 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 PPRVvac infection, seven succinylation motifs were identified. GO classification indicated that the differentially succinylated proteins (DSuPs) mainly participated in cellular respiration, biosynthetic process and transmembrane transporter activity. KEGG pathway analysis indicated that DSuPs were related to protein processing in the endoplasmic reticulum. Protein-protein interaction networks of the identified proteins provided further evidence that various 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.ConclusionsThe findings of the present study provide the first report of the succinylome in Vero cells infected with PPRVvac and provided a foundation for investigating the role of succinylation alone and its overlap with acetylation in response to PPRVvac.

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