Determination of a Unique Epitope Binding Site for a Complement-Lysis- Enhancing Monoclonal Antibody, 3D12, on the Galactose Adherence Lectin of Entamoeba histolytica, Using BIAcore.
Final rept. Jun-Sep 1991,
CHEMICAL RESEARCH DEVELOPMENT AND ENGINEERING CENTER ABERDEEN PROVING GROUND MD
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Mechanisms of pathogenicity used by Entamoeba histolytica to invade the bloodstream and cause liver abscess, include complement mediated lysis. Although pathogenic strains of E. histolytica become involved in immune functions by 1 activation of the alternate complement pathway, 2 binding of the C9 component of complement, and 3 depletion of active complement mediated hemolysis, the organism is not eliminated from the body by complement induced lysis. Monoclonal antibody mAb 3Dl2 vas produced to target molecules responsible for lysis resistance. Binding of mAb 3Dl2 to the galactose-specific surface lectin, circumvented resistance to C5b-9 complement lysis. The epitope position on the adherence lectin for mAb 3D12 vas mapped using BIAcore. Epitope specificity of mAb 3DI2 is unique and separate from six previously characterized monoclonal antibodies and plays a role in enhancing complement mediated lysis of E. histolytica. Complement mediated lysis, Pathogenicity, Epitope, Epitope specific monoclonal antibody, Adherence lectin.
- Medicine and Medical Research