N-linked oligosaccharides of cobra venom factor contain novel  (1-3)galactosylated Lex structures

Cobra venom factor (CVF), a nontoxic, complement-activating glycoprotein in cobra venom, is a functional analog of mammalian complement component C3b. The carbohydrate moiety of CVF consists exclusively of N-linked oligosaccharides with terminal [alpha]1-3-linked galactosyl residues, which are antig...

Full description

Saved in:
Bibliographic Details
Published in:Glycobiology (Oxford) 2001-03, Vol.11 (3), p.195-208
Main Authors: Gowda, D. C., Glushka, J., Halbeek, H. v., Thotakura, R. N., Bredehorst, R., Vogel, C.-W.
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Cobra venom factor (CVF), a nontoxic, complement-activating glycoprotein in cobra venom, is a functional analog of mammalian complement component C3b. The carbohydrate moiety of CVF consists exclusively of N-linked oligosaccharides with terminal [alpha]1-3-linked galactosyl residues, which are antigenic in human. CVF has potential for several medical applications, including targeted cell killing and complement depletion. Here, we report a detailed structural analysis of the oligosaccharides of CVF. The structures of the oligosaccharides were determined by lectin affinity chromatography, antibody affinity blotting, compositional and methylation analyses, and high-resolution 1H-NMR spectroscopy. Approximately 80% of the oligosaccharides are diantennary complex-type, ~12% are tri- and tetra-antennary complex-type, and ~8% are oligomannose type structures. The majority of the complex-type oligosaccharides terminate in Gal[alpha]1-3Gal[beta]1-4(Fuc[alpha]1-3)GlcNAc[beta]1, a unique carbohydrate structural feature abundantly present in the glycoproteins of cobra venom.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/11.3.195