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- N 4-( N-acetyl-β-glucosaminyl) asparagine amidase). The deglycosylation of CVF chains seems to proceed independentl...

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Veröffentlicht in:Molecular immunology 1989-06, Vol.26 (6), p.563-574
Hauptverfasser: Grier, Alice H., Vogel, Carl Wilhelm
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container_title Molecular immunology
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creator Grier, Alice H.
Vogel, Carl Wilhelm
description 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- N 4-( N-acetyl-β-glucosaminyl) asparagine amidase). The deglycosylation of CVF chains seems to proceed independently of each other, leading to partially deglycosylated intermediates. Complete deglyeosylation 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.
doi_str_mv 10.1016/0161-5890(89)90008-4
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subjects Animals
Biological and medical sciences
Complement
Complement Activation - drug effects
Elapid Venoms - pharmacology
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Glycoside Hydrolases - pharmacology
Glycosylation
Guinea Pigs
Humans
Molecular immunology
Oligosaccharides - pharmacology
title The oligosaccharide chains of cobra venom factor are required for complement activation
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