Global quantitative phosphoproteome reveals phosphorylation network of bovine lung tissue altered by Mycobacterium bovis
文献类型: 外文期刊
第一作者: Yu, Xi
作者: Yu, Xi;Yang, Wenmin;Stojkoska, Andrea;Xie, Jianping;Cheng, Guangyu;Yue, Ruichao;Wang, Jie;Liao, Yi;Sun, Xin;Zhou, Xiangmei;Liu, Chunfa;Yang, Hongjun
作者机构:
关键词: Bovine tuberculosis; Phosphoproteome; Glucose metabolism; Signal transducer and activator of transcription 3; Serine/arginine repetitive matrix protein 2; Insulin receptor substrate 1
期刊名称:MICROBIAL PATHOGENESIS ( 影响因子:3.738; 五年影响因子:3.663 )
ISSN: 0882-4010
年卷期: 2020 年 147 卷
页码:
收录情况: SCI
摘要: Bovine tuberculosis caused by Mycobacterium bovis remains a major cause of economic loss in cattle industries worldwide. However, the pathogenic mechanisms remain poorly understood. Post-translation modifications (PTM) such as phosphorylation play a crucial role in pathogenesis. While the change of transcriptome and proteome during the interaction between M. bovis and cattle were studied, there are no reports on the phosphoproteome change. We apply Tandem Mass Tag-based (TMT) quantitative proteomics coupled with immobilized metal-chelated affinity chromatography (IMAC) enrichment to obtain the quantified phosphorylation in vivo of M. bovis infected cattle lung tissue. The phosphorylated proteins are widespread in the nucleus, cytoplasm and plasma membrane. By using a change fold of 1.2, 165 phosphosites from 147 proteins were enriched, with 88 upregulated and 77 downregulated sites respectively. We further constructed the protein-protein interaction (PPI) networks of STAT3, SRRM2 and IRS-1 based on their number of differential phosphorylation sites and KEGG pathways. Similar patterns of gene expression dynamics of selected genes were observed in Mycobacterium tuberculosis infected human sample GEO dataset, implicating crucial roles of these genes in pathogenic Mycobacteria - host interaction. The first phosphorproteome reveals the relationship between bovine tuberculosis and glucose metabolism, and will help further refinement of target proteins for mechanistic study.
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