iTRAQ-Based Phosphoproteomic Analysis Exposes Molecular Changes in the Small Intestinal Epithelia of Cats after <i>Toxoplasma gondii</i> Infection
Bintao Zhai,
Yu-Meng Meng,
Shi-Chen Xie,
Jun-Jie Peng,
Yang Liu,
Yanhua Qiu,
Lu Wang,
Jiyu Zhang,
Jun-Jun He
Affiliations
Bintao Zhai
Key Laboratory of Veterinary Pharmaceutical Development, Lanzhou Institute of Husbandry and Pharma-Ceutical Sciences, Chinese Academy of Agricultural Sciences, Ministry of Agriculture and Rural Affairs, Lanzhou 730050, China
Yu-Meng Meng
State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Xujiaping 1, Lanzhou 730046, China
Shi-Chen Xie
College of Veterinary Medicine, Shanxi Agricultural University, Taigu, Jinzhong 030801, China
Jun-Jie Peng
State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Xujiaping 1, Lanzhou 730046, China
Yang Liu
College of Life Science, Ningxia University, Yinchuan 750021, China
Yanhua Qiu
Key Laboratory of Veterinary Pharmaceutical Development, Lanzhou Institute of Husbandry and Pharma-Ceutical Sciences, Chinese Academy of Agricultural Sciences, Ministry of Agriculture and Rural Affairs, Lanzhou 730050, China
Lu Wang
College of Veterinary Medicine, Shanxi Agricultural University, Taigu, Jinzhong 030801, China
Jiyu Zhang
Key Laboratory of Veterinary Pharmaceutical Development, Lanzhou Institute of Husbandry and Pharma-Ceutical Sciences, Chinese Academy of Agricultural Sciences, Ministry of Agriculture and Rural Affairs, Lanzhou 730050, China
Jun-Jun He
Key Laboratory of Veterinary Public Health of Yunnan Province, College of Veterinary Medicine, Yunnan Agricultural University, Kunming 650201, China
Toxoplasma gondii, an obligate intracellular parasite, has the ability to invade and proliferate within most nucleated cells. The invasion and destruction of host cells by T. gondii lead to significant changes in the cellular signal transduction network. One important post-translational modification (PTM) of proteins is phosphorylation/dephosphorylation, which plays a crucial role in cell signal transmission. In this study, we aimed to investigate how T. gondii regulates signal transduction in definitive host cells. We employed titanium dioxide (TiO2) affinity chromatography to enrich phosphopeptides in the small intestinal epithelia of cats at 10 days post-infection with the T. gondii Prugniuad (Pru) strain and quantified them using iTRAQ technology. A total of 4998 phosphopeptides, 3497 phosphorylation sites, and 1805 phosphoproteins were identified. Among the 705 differentially expressed phosphoproteins (DEPs), 68 were down-regulated and 637 were up-regulated. The bioinformatics analysis revealed that the DE phosphoproteins were involved in various cellular processes, including actin cytoskeleton reorganization, cell necroptosis, and MHC immune processes. Our findings confirm that T. gondii infection leads to extensive changes in the phosphorylation of proteins in the cat intestinal epithelial cells. The results of this study provide a theoretical foundation for understanding the interaction between T. gondii and its definitive host.
