The oligosaccharide chains of cobra venom factor are required for complement activation.
To examine the function of the carbohydrate chains of cobra venom factor (CVF), the molecule was enzymatically deglycosylated under non-denaturing conditions with N-glycanase (peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase). The deglycosylation of CVF chains seems to proceed independently of each other, leading to partially deglycosylated intermediates. Complete deglycosylation of CVF was found to abolish the activity of CVF. The deglycosylated molecule is unable to activate the alternative pathway of complement. Deglycosylated CVF no longer consumes the serum complement activity, it does not induce C3 activation in serum, nor does it induce complement-mediated hemolysis. These results indicate that the carbohydrate moieties of CVF are essential for its role in complement activation.
Department of Biochemistry, Georgetown University School of Medicine, Washington, DC 20007.
A H
AH
Grier
C W
CW
Vogel
D000818:Animals; D003167:Complement Activation / Q000187:drug effects*; D004546:Elapid Venoms / Q000494:pharmacology*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006031:Glycosylation; D006168:Guinea Pigs; D006801:Humans; D009844:Oligosaccharides / Q000494:pharmacology*
D004546:Elapid Venoms; D009844:Oligosaccharides; C016310:cobra venom factor; D006026:Glycoside Hydrolases; C020668:glycanase