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PXD026655

PXD026655 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGlobal Phosphoproteomics Analysis of IBRS-2 Cells Infected with Senecavirus A
DescriptionPhosphorylation is a widespread post-translational modification that regulates numerous biological processes. Viruses can alter the physiological activities of host cells to promote virus particle replication, and manipulating phosphorylation is one of the mechanisms. Senecavirus A (SVA) the causative agent of porcine idiopathic vesicular disease. Although numerous studies on SVA have been performed, comprehensive phosphoproteomics analysis of SVA infection is lacking. In the present study, we performed a quantitative mass spectrometry-based phosphoproteomics survey of SVA infection in instituto biologico-rim suino-2 (IBRS-2) cells. Three parallel experiments were performed and 4520 phosphosites were identified on 2084 proteins. Gene Ontology functional enrichment and Kyoto Encyclopedia of Genes and Genomes pathway enrichment analyses showed that many of the phosphorylated proteins were involved in apoptosis and spliceosome pathways, and subcellular structure localisation analysis revealed that more than half were located in the nucleus. Motif analysis of proteins with differentially regulated phosphosites showed that proline, aspartic acid and glutamic acid were the most abundant residues in the serine motif, while proline and arginine were the most abundant in the threonine motif. Forty phosphosites on 27 proteins were validated by parallel reaction monitoring phosphoproteomics, and 30 phosphosites in 21 proteins were verified. Nine proteins with significantly altered phosphosites were further explored, and eight (SRRM2, CDK13, DDX20, DDX21, BAD, ELAVL1, PBK, and STAT3) may play a role in SVA infection. Finally, identified eight predicted kinases, and the kinase activity of inhibitor of nuclear factor kappa-B kinase subunit β and CDK9 was reversed following SVA infection. This is the first phosphoproteomics analysis of SVA infection of IBRS-2 cells, and the results greatly expand our knowledge of SVA infection. The findings provide a basis for studying the interactions of other picornaviruses and their mammalian host cells.
HostingRepositoryPRIDE
AnnounceDate2022-02-22
AnnouncementXMLSubmission_2022-02-22_04:38:10.845.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJieyi Li
SpeciesList scientific name: Sus scrofa domesticus (domestic pig); NCBI TaxID: 9825;
ModificationListNo PTMs are included in the dataset
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-06-11 07:24:33ID requested
12022-02-22 04:38:11announced
Publication List
Li J, Zhang Z, Lv J, Ma Z, Pan L, Zhang Y, Global Phosphoproteomics Analysis of IBRS-2 Cells Infected With Senecavirus A. Front Microbiol, 13():832275(2022) [pubmed]
Keyword List
submitter keyword: Protein modification
phosphoproteome
bioinformatics, pathway analysis
protein kinases
Senecavirus AProtein modification
phosphoproteome
bioinformatics, pathway analysis
protein kinases
Senecavirus A
Contact List
Li Jieyi
contact affiliationLanzhou Veterinary Research Institute
contact emailmangranjie@163.com
lab head
Jieyi Li
contact affiliation1
contact emailmangranjie@163.com
dataset submitter
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