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Phosphoproteomics analysis of cat small intestine following Toxoplasma gondii infection

ABSTRACT: Toxoplasma gondii is an obligate intracellular parasite, which can invade most nucleated cells and proliferate inside the cells. During the process of T. gondii invasion and proliferate inside host cells, the cellular signal transduction network of the infected cells undergoing extensive changes. Phosphorylation is one of the most important post-translational modifications of proteins, and plays an important role in the process of cell signal transmission. To clarify how T. gondii regulates the host cell signal transduction process, in this study, we used titanium dioxide (TiO2) affinity chromatography to enrich the phosphopeptides in feline small intestine at 10 days post infection of T. gondii Prugniuad (Pru) strain, and quantify the phosphopeptides by using iTRAQ technology.

ORGANISM(S): Felis Catus

SUBMITTER: Xing-Quan Zhu

PROVIDER: PXD023322 | iProX | Mon Dec 28 00:00:00 GMT 2020

REPOSITORIES: iProX

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Project description:Phosphorylation is a regulatory mechanism by which intracellular apicomplexan parasites control the process of invading and modifying host cells. However, the sporulated oocysts’ phosphoprotein repertoires between virulent and avirulent strains of Toxoplasma gondii and the underlying mechanisms contributing to virulence is still a mystery. A quantitative analysis of the sporulated oocysts’ phosphoproteome profile of T. gondii virulent and avirulent strains belonging to different genotypes was conducted to reveal phosphoprotein expression patterns that contribute to the virulence of a particular phenotype. Phosphopeptides from the sporulated oocysts of the virulent strain PYS (Chinese ToxoDB#9) and the avirulent strain type II (PRU strain) were enriched by titanium dioxide (TiO2) affinity chromatography and quantified using iBT technology. A total of 10,645 unique phosphopeptides, 8,181 nonredundant phosphorylation sites and 2,792 phosphoproteins were identified. The quantitative analysis identified 4,129 differentially expressed phosphopeptides (DEPs) between sporulated oocysts of the PYS strain and PRU strain (|log1.5 fold change| > 1 and P < 0.05), including 2,485 upregulated and 1,644 downregulated phosphopeptides. Motif analysis identified 24 motifs from the upregulated phosphorylated peptides including 22 serine motifs and two threonine motifs (TPE and TP), and 15 motifs from the downregulated phosphorylated peptides including 12 serine motifs and three threonine motifs (TP, RxxT and KxxT) in PYS strain when comparing PYS/PRU. Several kinases were consistent with motifs of overrepresented phosphopeptides, such as PKA, PKG, CKII, IKK, MAPK, EGFR, INSR, Jak, Syk, Src, Ab1. GO analysis, KEGG pathway analysis and STRING analysis revealed differentially expressed phosphoproteins (DEPs) exhibiting significant functional properties. Kinase associated network analysis showed that AGC kinase had the greatest connected peptides. Our findings reveal significant difference in phosphopeptides of sporulated oocysts between virulent and avirulent T. gondii strains, which provides solid foundation for further exploring the mechanisms contributing to the virulence of T. gondii.

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Phosphoproteomics analysis of cat small intestine following Toxoplasma gondii infection

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