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Transcriptomics of Toxoplasma gondii sporulating oocysts

ABSTRACT: Toxoplasma gondii is an apicomplexan parasite that approximately infects one third of the human population worldwide. When sporulated oocysts that are shed in the faeces of infected felids are accidentally ingested through contaminated food or water, sporozoites can infect the intestine of the intermediate host. Upon this infection, the fast replicating tachyzoites then disseminate overall the body and can cross the blood-brain, blood-retina or the blood-placenta barrier. Eventually, immune pressure will lead to differentiation into the slow replicating bradyzoites that are contained within tissue cysts for life. Despite the importance of sporulation for transmission, the process is not yet understood. We therefore exploited Illumina Next-Generation RNA-Sequencing to analyse the transcriptome of oocysts in the process of sporulation and compared it to unsporulated and sporulated oocysts. We thus identified genes that are highly specific to the sporulation process and that may be involved in the formation of sporozoites.

ORGANISM(S): Toxoplasma gondii

PROVIDER: GSE206344 | GEO | 2022/06/20

REPOSITORIES: GEO

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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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Transcriptomics of Toxoplasma gondii sporulating oocysts

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