Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins

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• 作者：Chunsheng Jin ; J谩nos Tam谩s Padra ; Kristina Sundell ; Henrik Sundh ; Niclas G. Karlsson ; Sara K. Lind茅n
• 刊名：Journal of Proteome Research
• 出版年：2015
• 出版时间：August 7, 2015
• 年：2015
• 卷：14
• 期：8
• 页码：3239-3251
• 全文大小：849K
• ISSN：1535-3907

文摘

Aquaculture is a growing industry, increasing the need for understanding host鈥損athogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2鈥? residues) and less diverse (33 structures) than intestinal O-glycans (2鈥?3 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host鈥損athogen interactions for further testing in biological assays and disease intervention therapies.