Global profiling of protein S-palmitoylation in the second-generation merozoites of Eimeria tenella
文献类型: 外文期刊
作者: Qu, Zigang 1 ; Li, Yuqiong 4 ; Li, Wenhui 1 ; Zhang, Nianzhang 1 ; Olajide, Joshua Seun 1 ; Mi, Xiaoyun 5 ; Fu, Baoquan 1 ;
作者机构: 1.Chinese Acad Agr Sci, State Key Lab Anim Dis Control & Prevent, Lanzhou Vet Res Inst, Lanzhou 730046, Gansu, Peoples R China
2.Chinese Acad Agr Sci, Lanzhou Vet Res Inst, Minist Agr, Key Lab Vet Publ Hlth, Lanzhou 730046, Peoples R China
3.Chinese Acad Agr Sci, Lanzhou Vet Res Inst, Key Lab Vet Parasitol Gansu Prov, Lanzhou 730046, Gansu, Peoples R China
4.Ningxia Acad Agr & Forestry Sci, Yinchuan 750002, Peoples R China
5.Xinjiang Acad Anim Sci, Inst Vet Med, Xinjiang Key Lab Anim Infect Dis, Urumqi 830013, Xinjiang, Peoples R China
6.Jiangsu Coinnovat Ctr Prevent & Control Anim Infec, Yangzhou 225009, Jiangsu, Peoples R China
关键词: Protein acylation; E. tenella; Bioiological process; The second-generation merozoites
期刊名称:PARASITOLOGY RESEARCH ( 影响因子:2.0; 五年影响因子:2.0 )
ISSN: 0932-0113
年卷期: 2024 年 123 卷 4 期
页码:
收录情况: SCI
摘要: The intracellular protozoan Eimeria tenella is responsible for avian coccidiosis which is characterized by host intestinal damage. During developmental cycle, E. tenella undergoes versatile transitional stages such as oocyst, sporozoites, merozoites, and gametocytes. These developmental transitions involve changes in cell shape and cell size requiring cytoskeletal remodeling and changes in membrane proteins, which may require transcriptional and translational regulations as well as post-translational modification of proteins. Palmitoylation is a post-translational modification (PTM) of protein that orchestrates protein targeting, folding, stability, regulated enzymatic activity and even epigenetic regulation of gene expression. Previous research revealed that protein palmitoylation play essential role in Toxoplasma gondii, Trypanosoma cruzi, Trichomonas vaginalis, and several Plasmodium parasites. Until now, there is little information on the enzymes related to palmitoylation and role of protein acylation or palmitoylation in E. tenella. Therefore, palmitome of the second-generation merozoite of E. tenella was investigated. We identified a total of 2569 palmitoyl-sites that were assigned to 2145 palmitoyl-peptides belonging to 1561 protein-groups that participated in biological processes including parasite morphology, motility and host cell invasion. In addition, RNA biosynthesis, protein biosynthesis, folding, proteasome-ubiquitin degradation, and enzymes involved in PTMs, carbohydrate metabolism, glycan biosynthesis, and mitochondrial respiratory chain as well as vesicle trafficking were identified. The study allowed us to decipher the broad influence of palmitoylation in E. tenella biology, and its potential roles in the pathobiology of E. tenella infection. Raw data are publicly available at iProX with the dataset identifier PXD045061.
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