Comparative proteomic analysis of virulent and avirulent strains of Toxoplasma gondii reveals strain-specific patterns
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Dong-Hui Zhou1,*, Ze-Xiang Wang1,*, Chun-Xue Zhou1,3, Shuai He1,4, Hany M. Elsheikha2 and Xing-Quan Zhu1
1State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, Gansu Province, 730046, PR China
2Faculty of Medicine and Health Sciences, School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, UK
3Department of Parasitology, Shandong University School of Basic Medicine, Jinan, Shandong Province, 250012, PR China
4College of Animal Science and Technology, Anhui Agricultural University, Hefei, Anhui Province, 230036, PR China
*These authors contributed equally to this work
Hany M. Elsheikha, email: firstname.lastname@example.org
Xing-Quan Zhu, email: email@example.com
Keywords: Toxoplasma gondii, oocyst, proteomics, iTRAQ, differentially expressed protein (DEP)
Received: April 18, 2017 Accepted: June 18, 2017 Published: July 07, 2017
Research exploring the proteome of Toxoplasma gondii oocysts has gained momentum over the past few years. However, little is known about the oocyst’s protein repertoires that contribute to differential virulence among T. gondii strains. Here, we used isobaric tag for relative and absolute quantitation-based proteomic analysis of oocysts of two T. gondii strains exhibiting the virulent PYS (ToxoDB#9) phenotype versus the less virulent PRU (Type II, ToxoDB#1) phenotype. Our aim was to determine protein expression patterns that contribute to the virulence of a particular phenotype. A total of 2,551 proteins were identified, of which 374 were differentially expressed proteins (DEPs) (|log2 fold change| ≥ 0.58 and P < 0.05). DEPs included 192 increased and 182 decreased proteins. Gene Ontology and KEGG pathway analyses revealed a large number of DEPs enriched in various metabolic processes. Protein interaction network analysis using STRING identified inosine monophosphate dehydrogenase (IMPDH), Bifunctional GMP synthase/glutamine amidotransferase protein, Glucose-6-phosphate 1-dehydrogenase, and Citrate synthase as the top four hubs. Of the 22 virulence proteins commonly expressed in the oocysts of the two strains, 13 and 2 proteins were increased in PYS strain and PRU strain, respectively. Also, 10 and 3 of the 22 identified oocyst wall proteins showed higher expression in oocysts of PRU strain and PYS strain, respectively. These findings revealed new proteomic differences in the oocysts of T. gondii strains of different genotypic backgrounds.
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