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

• 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 S 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.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

Atlantic salmon

fish

O-glycan

mucins

skin

gastrointestinal tract

mucus

glycosylation

RAINBOW-TROUT

OLIGOSACCHARIDE-ALDITOLS

MISGURNUS-ANGUILLICAUDATUS

ONCORHYNCHUS-MYKISS

JELLY COATS

MUC2 MUCIN

ZEBRAFISH

GLYCOPROTEIN

GLYCOSYLATION

CHAINS

Biochemical Research Methods

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