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Bisecting Galactose as a Feature of N-Glycans of Wild-type and Mutant Caenorhabditis elegans
- Source :
- Molecularcellular proteomics : MCP. 14(8)
- Publication Year :
- 2015
-
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 α-mannosidase-resistant N-glycans. Within this glycomic subpool, we can reveal that the core β-mannose can be trisubstituted and so carries not only the ubiquitous α1,3- and α1,6-mannose residues, but also a “bisecting” β-galactose, which is substoichiometrically modified with fucose or methylfucose. In addition, the α1,3-mannose can also be α-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.
- Subjects :
- Glycan
Proteome
Proton Magnetic Resonance Spectroscopy
Mutant
Biochemistry
Methylation
Fucose
Analytical Chemistry
chemistry.chemical_compound
Gene Knockout Techniques
Isomerism
Polysaccharides
Tandem Mass Spectrometry
Mannosidases
Animals
Protein Isoforms
Caenorhabditis elegans
Molecular Biology
Gene
Fucosylation
Chromatography, High Pressure Liquid
Glycoproteins
Chromatography, Reverse-Phase
biology
Research
Wild type
Galactose
biology.organism_classification
Fucosyltransferases
chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Mutation
biology.protein
Subjects
Details
- ISSN :
- 15359484
- Volume :
- 14
- Issue :
- 8
- Database :
- OpenAIRE
- Journal :
- Molecularcellular proteomics : MCP
- Accession number :
- edsair.doi.dedup.....0a962c6d4e73d05dda937f71af73d841