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Comparisons of Caenorhabditis Fucosyltransferase Mutants Reveal a Multiplicity of Isomeric N-Glycan Structures

Journal article
Authors S. Yan
Chunsheng S. Jin
I. B. H. Wilson
K. Paschinger
Published in Journal of Proteome Research
Volume 14
Issue 12
Pages 5291-5305
ISSN 1535-3893
Publication year 2015
Published at Institute of Biomedicine
Pages 5291-5305
Language en
Links dx.doi.org/10.1021/acs.jproteome.5b...
Keywords bisect, fucosyltransferase mutant, glycomics, nematode, SUBSTRATE-SPECIFICITY, HAEMONCHUS-CONTORTUS, LINKED GLYCANS, WILD-TYPE, ELEGANS, OLIGOSACCHARIDES, GLYCOSYLATION, CORE, BIOSYNTHESIS, COMPLEXITY, Biochemical Research Methods, ATES OF AMERICA, V111, PE2787
Subject categories Biochemistry and Molecular Biology

Abstract

Recent studies have shown a remarkable degree of plasticity in the N-glycome of the model nematode Caenorhabditis elegans; ablation of glycosylation-relevant genes can result in radically altered N-glycan profiles despite only minor biological phenotypic effects. Up to four fucose residues and five different linkages of fucose are known on the N-glycans of C. elegans. Due to the complexity in the wild type, we established three mutant strains defective in two core fucosyltransferases each (fut-1;fut-6, fut-1;fut-8, and fut-6;fut-8). Enzymatically released N-glycans were subject to HPLC and MALDI-TOF MS/MS, in combination with various treatments, to verify structural details. The N-glycome of the fut-1;fut-6 mutant was the most complex of the three double-mutant strains due to the extension of the core alpha 1,6-fucose as well as the presence of fucose on the bisecting galactose. In contrast, maximally two fucoses were found on N-glycans of the fut-1;fut-8 and fut-6;fut-8 strains. The different locations and capping of fucose meant that up to 13 isomeric structures, many highly galactosylated, were determined for some single masses. These data not only show the high variability of the N-glycomic capacity of a "simple" nematode but also exemplify the need for multiple approaches to reveal individual glycan structures within complex invertebrate glycomes.

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