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Bisecting Galactose as a Feature of N-Glycans of Wild-type and Mutant Caenorhabditis elegans

Journal article
Authors S. Yan
L. Brecker
Chunsheng S. Jin
A. Titz
M. Dragosits
Niclas G. Karlsson
V. Jantsch
I. B. H. Wilson
K. Paschinger
Published in Molecular & Cellular Proteomics
Volume 14
Issue 8
Pages 2111-2125
ISSN 1535-9476
Publication year 2015
Published at Institute of Biomedicine
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 2111-2125
Language en
Links dx.doi.org/10.1074/mcp.M115.049817
Keywords LINKED OLIGOSACCHARIDES, HAEMONCHUS-CONTORTUS, HYGIENE HYPOTHESIS, MODEL, ORGANISMS, CORE STRUCTURES, TRICHURIS-SUIS, NEMATODE, COMPLEX, PARASITES, GLYCOSYLATION, Biochemical Research Methods
Subject categories Biochemistry and Molecular Biology

Abstract

The N-glycosylation of the model nematode Caenorhabditis elegans has proven to be highly variable and rather complex; it is an example to contradict the existing impression that "simple" organisms possess also a rather simple glycomic capacity. In previous studies in a number of laboratories, N-glycans with up to four fucose residues have been detected. However, although the linkage of three fucose residues to the N,N'-diacetylchitobiosyl core has been proven by structural and enzymatic analyses, the nature of the fourth fucose has remained uncertain. By constructing a triple mutant with deletions in the three genes responsible for core fucosylation (fut-1, fut-6 and fut-8), we have produced a nematode strain lacking products of these enzymes, but still retaining maximally one fucose residue on its N-glycans. Using mass spectrometry and HPLC in conjunction with chemical and enzymatic treatments as well as NMR, we examined a set of alpha-mannosidase-resistant N-glycans. Within this glycomic sub-pool, we can reveal that the core beta-mannose can be trisubstituted and so carries not only the ubiquitous alpha 1,3- and alpha 1,6-mannose residues, but also a "bisecting" alpha-galactose, which is substoichiometrically modified with fucose or methylfucose. In addition, the alpha 1,3-mannose can also be alpha-galactosylated. Our data, showing the presence of novel N-glycan modifications, will enable more targeted studies to understand the biological functions and interactions of nematode glycans.

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