N-linked oligosaccharides of cobra venom factor contain novel [alpha](1-3)galactosylated Lex structures.
Gowda, D. Channe 1,5; Glushka, John 6; van Halbeek, Herman 2,6; Thotakura, Rao N. 7; Bredehorst, Reinhard 3,5; Vogel, Carl-Wilhelm 4,5
[Article]
Glycobiology.
11(3):195-208, March 2001.
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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.
(C) Copyright Oxford University Press 2001.