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

C Jin, JT Padra, K Sundell, H Sundh… - Journal of proteome …, 2015 - ACS Publications
C Jin, JT Padra, K Sundell, H Sundh, NG Karlsson, SK Lindén
Journal of proteome research, 2015ACS Publications
Aquaculture is a growing industry, increasing the need for understanding host–pathogen
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 …
Aquaculture is a growing industry, increasing the need for understanding host–pathogen 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 (2–6 residues) and less diverse (33 structures) than intestinal O-glycans (2–13 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–pathogen interactions for further testing in biological assays and disease intervention therapies.
ACS Publications