Year-end Sale % OFF 
Abstract
Toxoplasma gondii is an obligate intracellular protozoan of severe threat to humans and livestock, whose life history harbors both gamic and apogamic stages. Chinese 1 (ToxoDB#9) was a preponderant genotype epidemic in food-derived animals and humans in China, with a different pathogenesis from the strains from the other nations of the world. Posttranslational modifications (PTMs) of proteins were critical mediators of the biology, developmental transforms, and pathogenesis of protozoan parasites. The phosphoprotein profiling and the difference between the developmental phases of T. gondii, contributing to development and infectivity, remain unknown. A quantitative phosphoproteomic approach using IBT integrated with TiO2 affinity chromatography was applied to identify and analyze the difference in the phosphoproteomes between the sporulated oocysts and the tachyzoites of the virulent ToxoDB#9 (PYS) strain of T. gondii. A total of 4058 differential phosphopeptides, consisting of 2597 upregulated and 1461 downregulated phosphopeptides, were characterized between sporulated the oocysts and tachyzoites. Twenty-one motifs extracted from the upregulated phosphopeptides contained 19 serine motifs and 2 threonine motifs (GxxTP and TP), whereas 16 motifs identified from downregulated phosphopeptides included 13 serine motifs and 3 threonine motifs (KxxT, RxxT, and TP). Beyond the traditional kinases, some infrequent classes of kinases, including Ab1, EGFR, INSR, Jak, Src and Syk, were found to be corresponding to motifs from the upregulated and downregulated phosphopeptides. Remarkable functional properties of the differentially expressed phosphoproteins were discovered by GO analysis, KEGG pathway analysis, and STRING analysis. S8GFS8 (DNMT1-RFD domain-containing protein) and S8F5G5 (Histone kinase SNF1) were the two most connected peptides in the kinase-associated network. Out of these, phosphorylated modifications in histone kinase SNF1 have functioned in mitosis and interphase of T. gondii, as well as in the regulation of gene expression relevant to differentiation. Our study discovered a remarkable difference in the abundance of phosphopeptides between the sporulated oocysts and tachyzoites of the virulent ToxoDB#9 (PYS) strain of T. gondii, which may provide a new resource for understanding stage-specific differences in PTMs and may enhance the illustration of the regulatory mechanisms contributing to the development and infectivity of T. gondii.
Highlights
Toxoplasma gondii is a monocellular and intracellular protozoa that obligately subsists in host cells
To gain a deeper understanding of the differences between the mature oocysts and tachyzoites of T. gondii, we used a quantitative phosphoproteomic approach based on isobaric tag (IBT) to compare the phosphoproteomes of mature oocysts and tachyzoites of the virulent
A total of 8181 nonredundant phosphorylation sites and 2792 phosphoproteins were characterized from the mature oocysts and tachyzoites of the virulent T. gondii pure cyst of the virulent ToxoDB#9 (PYS) strain based on an false discovery rate (FDR) below 0.01 for phosphopeptides and a phosphoRS possibility above 0.75 for phosphosites
Summary
Toxoplasma gondii is a monocellular and intracellular protozoa that obligately subsists in host cells. Three major clonal lineages, which were referred to as subtypes I, II, and III, were found in North America and Europe in history [4]. Most of the strains isolated from wildlife in North America were designated as type 12, the fourth subtype [5]. Studies of the epidemiological distribution involving T. gondii isolated from food-derived animals and humans in China revealed Chinese 1 (ToxoDB#9) was the predominant genotype, and this genotype harbored two virulent factors, GRA15II and ROP16I/III. The two virulent factors were diverse in the type I, II, and III strains of T. gondii. This suggested the pathogenesis of the Chinese
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
