PXD026655

PXD026655 is an original dataset announced via ProteomeXchange.

Title	Global Phosphoproteomics Analysis of IBRS-2 Cells Infected with Senecavirus A
Description	Phosphorylation 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.
HostingRepository	PRIDE
AnnounceDate	2022-02-22
AnnouncementXML	Submission_2022-02-22_04:38:10.845.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jieyi Li
SpeciesList	scientific name: Sus scrofa domesticus (domestic pig); NCBI TaxID: 9825;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2021-06-11 07:24:33	ID requested
⏵ 1	2022-02-22 04:38:11	announced

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]

submitter keyword: Protein modification

phosphoproteome

bioinformatics, pathway analysis

protein kinases

Senecavirus AProtein modification

phosphoproteome

bioinformatics, pathway analysis

protein kinases

Senecavirus A

Li Jieyi
contact affiliation	Lanzhou Veterinary Research Institute
contact email	mangranjie@163.com
lab head
Jieyi Li
contact affiliation	1
contact email	mangranjie@163.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD026655
     1. Label: PRIDE project
     2. Name: Global Phosphoproteomics Analysis of IBRS-2 Cells Infected with Senecavirus A