Glycobiology Advance Access originally published online on June 2, 2004
Glycobiology 2004 14(9):767-774; doi:10.1093/glycob/cwh105
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Glycobiology vol. 14 no. 9 © Oxford University Press 2004; all rights reserved.
Structural characterization of the N-glycan moiety and site of glycosylation in vitellogenin from the decapod crustacean Cherax quadricarinatus
3 Institute for Medical Physics and Biophysics University of Münster, Robert-Koch-Str. 31 D-48149, Münster, Germany; 4 Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; 5 Department of Life Sciences and the Institute for Applied Biosciences, Ben Gurion University, P.O. Box 653, Beer Sheva, Israel
Received on February 17, 2004; revised on May 26, 2004; accepted on May 27, 2004
Glycosylation is of importance for the structure and function of proteins. In the case of vitellin (Vt), a ubiquitous protein 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 synthesized 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 10 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 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.
2 Present address: Ecole Polytechnique Fédérale de Lausanne, EPFL-BCH-LCOM, CH-1015 Lausanne, Switzerland
1 To whom correspondence should be addressed; e-mail: isam.khalaila{at}epfl.ch
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