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

Artikel i vetenskaplig tidskrift
Författare S. Yan
L. Brecker
Chunsheng S. Jin
A. Titz
M. Dragosits
Niclas G. Karlsson
V. Jantsch
I. B. H. Wilson
K. Paschinger
Publicerad i Molecular & Cellular Proteomics
Volym 14
Nummer/häfte 8
Sidor 2111-2125
ISSN 1535-9476
Publiceringsår 2015
Publicerad vid Institutionen för biomedicin
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 2111-2125
Språk en
Länkar dx.doi.org/10.1074/mcp.M115.049817
Ämnesord LINKED OLIGOSACCHARIDES, HAEMONCHUS-CONTORTUS, HYGIENE HYPOTHESIS, MODEL, ORGANISMS, CORE STRUCTURES, TRICHURIS-SUIS, NEMATODE, COMPLEX, PARASITES, GLYCOSYLATION, Biochemical Research Methods
Ämneskategorier Biokemi och molekylärbiologi

Sammanfattning

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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