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The oligosaccharide chains of cobra venom factor are required for complement activation
1Department of Biochemistry, Georgetown University School of Medicine, Washington, DC 20007.
Molecular Immunology
|June 1, 1989
Summary
The carbohydrate chains of cobra venom factor (CVF) are essential for its function in activating the complement system. Removing these sugar chains completely stops CVF
Area of Science:
- Biochemistry
- Immunology
- Glycobiology
Background:
- Cobra venom factor (CVF) is a potent activator of the alternative pathway of complement.
- The functional role of carbohydrate moieties in CVF's activity remains unclear.
Purpose of the Study:
- To investigate the specific function of carbohydrate chains in cobra venom factor (CVF).
- To determine if deglycosylation affects CVF's ability to activate the complement system.
Main Methods:
- Enzymatic deglycosylation of CVF using N-glycanase under non-denaturing conditions.
- Assessing the impact of deglycosylation on CVF's complement-activating properties, including C3 activation and serum hemolysis.
Main Results:
- Deglycosylation proceeded independently for different CVF carbohydrate chains, forming intermediate products.
- Complete deglycosylation abolished CVF activity, rendering it unable to activate the alternative complement pathway.
- Deglycosylated CVF did not consume serum complement, induce C3 activation, or mediate hemolysis.
Conclusions:
- The carbohydrate moieties of CVF are critical for its biological function in complement activation.
- Glycosylation is essential for CVF's ability to initiate and sustain the alternative complement pathway.