Dataset Information

Systematic Analysis of Lysine Succinylation in Vero cell infected with small ruminant morbillivirus

ABSTRACT: Small ruminant morbillivirus (SRMV), formerly named Peste-des-petits ruminanats virus (PPRV), belongs to the genus Morbillivirus genus in the family Paramyxoviridae and leads to a highly contagious disease in small ruminants, especially goats and sheep. Lysine succinylation is a newly identified and conserved modification and plays important roles in host cells response to pathogen infection. Herein, we present the comprehensive analysis of the succinylome of SRMV-infected Vero cell using quantitative proteomics. Overall, we identified 875 succinylated proteins with 2840 succinylation sites. Comparative analysis revealed that 139 down-regulated succinylated proteins with 228 succinylation sites and 38 up-regulated succinylated proteins with 44 succinylation sites were significant succinylated in response to SRMV infection, seven lysine succinylation motifs were identified. Bioinformatics analysis showed that the succinalated proteins mainly participated in 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, the overlapped proteins between succinylation and acetylation are involved in glyoxylate and dicarboxylate metabolism. In summary, this is the first study of the succinylome in SRMV infection, lysine acetylation may have a more important eﬀect than succinylation in PPRV infection. It provides a novel view on investigating the infection mechanism of SRMV.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Chlorocebus Sabaeus

TISSUE(S): Kidney Cell Line

SUBMITTER: xuelian meng

LAB HEAD: Xuelian meng

PROVIDER: PXD025025 | Pride | 2025-05-06

REPOSITORIES: Pride

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			Action	DRS
	Z8108TPSc01_rep1.raw	Raw
	Z8108TPSc01_rep1_combined.rar	Other
	Z8108TPSc01_rep1_mqpar.xml	Xml
	Z8108TPSc01_rep2.raw	Raw
	Z8108TPSc01_rep2_combined.rar	Other

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Publications

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

Meng Xuelian X Zhu Xueliang X Wang Xiangwei X Zhang Rui R Zhang Zhidong Z Sun Yuefeng Y

BMC veterinary research 20250130 1

<h4>Background</h4>Peste 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 re ...[more]

PMID: 39885502

Similar Datasets

Project description:Background Hypothyroidism is a common disease, and its molecular mechanism still needs further investigation. Succinylation, as a newly identified protein posttranslational modification, is found to be involved in various metabolisms and cellular processes. In the present study, we performed quantitative analysis of the lysine succinylome in the thyroid of rats with hypothyroxinemia. Methods Hypothyroxinemia was induced in rats through the administration of a high-fat diet and then the thyroid tissues were taken out for further analysis. Affinity enrichment and liquid chromatography-tandem mass spectrometry techniques were applied for the quantitative proteome and succinylome analyses, respectively. Bioinformatic analyses were performed to decipher the differentially expressed proteins and succinylated sites, including the gene ontology (GO) annotation-based classification, Wolfpsort-based subcellular localization prediction, Kyoto Encyclopedia of Genes and Genomes (KEGG)-based functional pathway enrichment, and conserved domains of protein and succinylation sites prediction. Finally, the mitochondrial oxygen consumption rates of human normal thyroid epithelial cells were measured to further verify the role of lysine succinylation in vitro. Results Overall, 3869 proteins were identified, among which 129 differentially expressed proteins were quantified. Downregulated expressed proteins were enriched in the thyroid hormone synthesis and thyroid hormone signaling pathways and were mainly localized to the mitochondria and ATPase complex. In addition, 685 lysine succinylation sites on 250 proteins were identified, of which 172 lysine succinylation sites on 104 proteins were obvious changed (7 upregulated on 5 proteins and 165 downregulated on 99 proteins). Decreased succinylated proteins were involved in diverse metabolic pathways and biological processes, including the tricarboxylic acid cycle (TCA cycle), cellular respiration, energy derivation by oxidation of organic compounds and aerobic respiration. Moreover, these decreased succinylated proteins were primarily localized to the mitochondria. Finally, OCRs related to basal respiration, ATP production and maximal respiration were markedly blunted in the normal thyroid epithelial cells treated with palmitic acid (all p < 0.05), and the changes were reversed when the cells were treated with palmitic acid and desuccinylase inhibitor together (all p < 0.05). Conclusions The thyroid differentially expressed proteins and changed succinylation levels played a potential role in the mitochondria-mediated energy metabolism in the HFD-induced hypothyroxinemia rat model.

Project description:Background: Lysine succinylation is a newly identified PTM, which exists widely from prokaryotes to eukaryotes and participates in various cellular processes, especially in the metabolic processes. Staphylococcus epidermidis is a commensal bacterium in the skin, which attracts more attention as a pathogen, especially in immunocompromised patients and neonates by attaching to medical devices and forming biofilms. However, the significance of lysine succinylation in proteins of Staphylococcus epidermidis has not been investigated. Materials and methods: Using antibody affinity enrichment followed by LC-MS/MS analysis, we examined the succinylome of Staphylococcus epidermidis (ATCC®12228™). Then, bioinformatics analysis was performed, including Gene Ontology, KEGG enrichment, motif characterization, secondary structure, protein-protein interaction, and BLAST analysis. Results: A total of 1557 succinylated lysine sites in 649 proteins were identified in Staphylococcus epidermidis (ATCC 12228). Among these succinylation proteins, GO annotation showed that proteins related to metabolic processes and binding activity accounted for the most based on the analysis of biological process and molecular function, respectively. KEGG pathway characterization indicated that proteins associated with the glycolysis/ gluconeogenesis, and citrate cycle (TCA cycle) pathway were more likely to be succinylated. Moreover, 13 conserved motifs were identified. The specific motif KsuD was conserved in model prokaryotes and eukaryotes. Succinylated proteins with this motif were highly enriched in the glycolysis/gluconeogenesis pathway. One succinylation site(K144) was identified in S-ribosylhomocysteine lyase, a key enzyme in the quorum sensing system, indicating the regulatory role succinylation may play in bacterial processes. Furthermore, 15 succinyltransferases and 18 desuccinylases(erasers) were predicted in S.epidermidis by BLAST analysis. Conclusions: We performed the first comprehensive profile of succinylation in Staphylococcus epidermidis and illustrated the significant role succinylation may play in energy metabolism, QS system, and other bacterial behaviors. This study may be a fundamental basis to investigate the underlying mechanisms of colonization, virulence, and infection of S. epidermidis, as well as provide a new insight into regulatory effects succinylation may lay on metabolic processes.