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N-glycan moieties of the crustacean egg yolk protein and their glycosylation sites

Content Provider	Springer Nature Link
Author	Roth, Ziv Parnes, Shmuel Wiel, Simy Sagi, Amir Zmora, Nili Chung, J. Sook Khalaila, Isam
Copyright Year	2009
Abstract	Vitellogenin (Vg) is the precursor of the egg yolk glycoprotein of crustaceans. In the prawn Macrobrachium rosenbergii, Vg is synthesized in the hepatopancreas, secreted to the hemolymph, and taken up by means of receptor-mediated endocytosis into the oocytes. The importance of glycosylation of Vg lies in its putative role in the folding, processing and transport of this protein to the egg yolk and in the fact that the N-glycan moieties could provide a source of carbohydrate during embryogenesis. The present study describes, for the first time, the structure of the glycan moieties and their sites of attachment to the Vg of M. rosenbergii. Bioinformatics analysis revealed seven putative N-glycosylation sites in M. rosenbergii Vg; two of these glycosylation sites are conserved throughout the Vgs of decapod crustaceans from the Pleocyemata suborder (N 159 and N 660). The glycosylation of six putative sites of M. rosenbergii Vg (N 151, N 159, N ,168 N ,614 N 660 and N 2300) was confirmed; three of the confirmed glycosylation sites are localized around the N-terminally conserved N-glycosylation site N 159. From a theoretical three-dimensional structure, these three N-glycosylated sites N 151, N 159, and N 168 were localized on the surface of the Vg consensus sequence. In addition, an uncommon high mannose N-linked oligosaccharide structure with a glucose cap (Glc1Man9GlcNAc2) was characterized in the secreted Vg. These findings thus make a significant contribution to the structural elucidating of the crustacean Vg glycan moieties, which may shed light on their role in protein folding and transport and in recognition between Vg and its target organ, the oocyte.
Starting Page	159
Ending Page	169
Page Count	11
File Format	PDF
ISSN	02820080
Journal	Glycoconjugate Journal
Volume Number	27
Issue Number	1
e-ISSN	15734986
Language	English
Publisher	Springer US
Publisher Date	2009-11-18
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Crustacea Glucose cap Glycosylation sites N-glycan Vitellogenin Pathology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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