Abstract
Phosphorylation is a widespread posttranslational 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) is the causative agent of porcine idiopathic vesicular disease. Although numerous studies on SVA have been performed, comprehensive phosphoproteomics analysis of SVA infection is lacking. The present study 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 4,520 phosphosites were quantified on 2,084 proteins. Gene Ontology (GO) functional enrichment and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analyses showed that many phosphorylated proteins were involved in apoptosis and spliceosome pathways, and subcellular structure localization 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 (PRM) phosphoproteomics, and 30 phosphosites in 21 proteins were verified. Nine proteins with significantly altered phosphosites were further discussed, and eight [SRRM2, CDK13, DDX20, DDX21, BAD, ELAVL1, PDZ-binding kinase (PBK), and STAT3] may play a role in SVA infection. Finally, kinase activity prediction showed 10 kinases’ activity was reversed following SVA infection. It 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.
Highlights
Senecavirus A (SVA), formerly known as Seneca Valley virus (SVV), is known for its selective tropism toward cancers and belongs to the genus Senecavirus, family Picornaviridae
Around 9 hpi was chosen as the optimal time for SVA infection of Instituto Biologico-Rim Suino-2 (IBRS-2) cells for the number of infected cells increased after
Global Detection of Phosphosites in IBRS-2 Cells Infected With SVA
Summary
Senecavirus A (SVA), formerly known as Seneca Valley virus (SVV), is known for its selective tropism toward cancers and belongs to the genus Senecavirus, family Picornaviridae. The first reported SVA, named SVV-001 in 2002, was identified incidentally as a contaminant in cultured PER.C6 cells (Adams et al, 2015). Since 2014, outbreaks of SVA-associated vesicular diseases in pigs have occurred in many countries worldwide (Zhu et al, 2017b; Saeng-Chuto et al, 2018). The first report of SVA infection in China was in 2015 (Zhu et al, 2017b). As an emerging infectious disease in pigs, the potential impact of SVA could be significant, and research is needed
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