Discovery and structural characterization of fucosylated oligomannosidic N-glycans in mushrooms |
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Authors: | Grass Josephine Pabst Martin Kolarich Daniel Pöltl Gerald Léonard Renaud Brecker Lothar Altmann Friedrich |
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Affiliation: | Department of Chemistry, University of Natural Resources and Life Sciences, 1190 Vienna, Austria. |
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Abstract: | L-fucose is a common constituent of Asn-linked glycans in vertebrates, invertebrates, and plants, but in fungal glycoproteins, fucose has not been found so far. However, by mass spectrometry we detected N-glycans and O-glycans containing one to six deoxyhexose residues in fruit bodies of several basidiomycetes. The N-glycans of chanterelles (Cantharellus cibarius) contained a deoxyhexose chromatographically identical to fucose and sensitive to α-L-fucosidase. Analysis of individual glycan species by tandem MS, glycosidase digestion, and finally (1)H NMR revealed the presence of L-fucose in α1,6-linkage to an α1,6-mannose of oligomannosidic N-glycans. The substitution by α1,6-mannose of α1,2-mannosyl residues of the canonical precursor structure was yet another hitherto unknown modification. No indication for the occurrence of yet other modifications, e.g. bisecting N-acetylglucosamine, was seen. Besides fucosylated N-glycans, short O-linked mannan chains substituted with fucose were present on chanterelle proteins. Although undiscovered so far, L-fucose appears to represent a prominent feature of protein-linked glycans in the fungal kingdom. |
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Keywords: | Fungi Glycoprotein Glycoprotein Structure NMR Post-translational Modification Chanterelle Fucose N-Glycan |
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