Proteomics and pathway analysis of N-glycosylated mammary gland proteins in response to Escherichia coli mastitis in cattle
文献类型: 外文期刊
作者: Yang, Yongxin 1 ; Shen, Weijun 2 ; Zhao, Xiaowei 1 ; Zhao, Huiling 1 ; Huang, Dongwei 1 ; Cheng, Guanglong 1 ;
作者机构: 1.Anhui Acad Agr Sci, Inst Anim Sci & Vet Med, Hefei 230031, Peoples R China
2.Hunan Agr Univ, Coll Anim Sci & Technol, Changsha 410128, Hunan, Peoples R China
关键词: Dairy cow;Mastitis;Escherichia coli;Glycosylation;Proteome
期刊名称:VETERINARY JOURNAL ( 影响因子:2.688; 五年影响因子:2.857 )
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收录情况: SCI
摘要: The aim of this study was to investigate the N-linked glycosylated protein profile of mammary tissue from healthy cows and cows with mastitis due to Escherichia coli, in order to understand the molecular mechanisms of the host response to mastitis. N-glycopeptides were enriched with a lectin mixture and identified through high-accuracy mass spectrometry. A total of 551 N-glycosylation sites, corresponding to 294 proteins, were identified in the mammary tissues of healthy cows; these glycoproteins were categorised into three functional groups and clustered into 11 specific pathways. A total of 511 N-glycosylation sites, corresponding to 283 glycosylated proteins, were detected in the mammary tissues of cows with E. coli mastitis. There were differences in N-glycosylation sites in 98 proteins in the mammary tissues of healthy cows and cows with mastitis due to E. coli. Most proteins with altered glycosylation were those involved in responses to stress, cell adhesion and the immune response, and were assigned to five specific pathways based on their gene ontology annotation. The results from this study show that the glycosylated protein profile in the mammary tissues of healthy and mastitic cows are different, and altered glycoproteins are associated with several pathways, including the lysosome and O-glycan biosynthesis pathways
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