Glycobiology Advance Access published online on June 2, 2004
Glycobiology, doi:10.1093/glycob/cwh105
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1 Institute for Medical Physics and Biophysics University of Münster, Robert-Koch-Str. 31 D-48149, Münster, Germany
* To whom correspondence should be addressed. E-mail: isam.khalaila{at}epfl.ch.
Glycosylation is of importance for the structure and function of proteins. In the case of vitellin (Vt), an ubiquitous protein that is accumulated into granules as the main yolk protein constituent of oocytes during oogenesis, glycosylation could be of importantance for the folding, processing and transport of the protein to the yolk and also provides a source of carbohydrate during embryogenesis. Vt from the crayfish Cherax quadricarinatus is synthesised as a precursor protein, vitellogenin (Vg), in the hepatopancreas, transferred to the hemolymph and mobilized into the growing oocyte via receptor-mediated endocytosis. The gene sequence of C. quadricarinatus shows a 2584 amino acid protein with ten putative glycosylation sites. In this study a combined approach of lectin immunoblotting, in-gel deglycosylation and mass spectrometry was used to identify the glycosylation sites and to probe the structure of the glycan moieties using C. quadricarinatus Vg as a model system. Three of the consensus sites for N-glycosylation, namely Asn152, Asn160 and Asn2493, were glycosylated with the high mannose glycans, Man5-9GlcNAc2 and the glucose capped oligosaccharide Glc1Man9GlcNAc2.
Revised May 26, 2004
Accepted May 27, 2004
ORIGINAL ARTICLES
Structural characterization of the N-glycan moiety and site of glycosylation in vitellogenin from the decapod crustacean Cherax quadricarinatus
2 Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
3 Department of Life Sciences, Ben Gurion University, P.O. Box 653, Beer Sheva, Israel; The Institute for Applied Biosciences, Ben Gurion University, P.O. Box 653, Beer Sheva, Israel
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