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Topologic mapping of protective and nonprotective epitopes on the variant surface glyco protein of the walter reed army trypanozoon antigen type 1 clone of trypanosoma brucei rhodesiense



Topologic mapping of protective and nonprotective epitopes on the variant surface glyco protein of the walter reed army trypanozoon antigen type 1 clone of trypanosoma brucei rhodesiense



Journal of Immunology 132(4): 2059-2063



Monoclonal antibodies were used in the competitive antibody binding assays to define and map epitopes on the variant surface glycoprotein of the WRATat 1 clone of T. bruce rhodesiense. By using panel of 30 WRATat 1-specific monoclonal antibodies, 16 epitopes were defined that fall into 4 clusters, having 1, 1, 3, and 11 distinct epitopes, respectively. All epitopes were easily classified as being exposed uniformly on the surface of the trypanosome, exposed only in the region of the flagellar pocket, or buried, based on the ability or inability of the monoclonal antibodies to bind living trypanosomes in a fluid phase immunofluorescence assay. Monoclonal antibodies that bind exposed surface epitopes are protective; only 3 of 7 that bind exclusively to flagellar pocket epitopes are protective. None of the 9 monoclonal antibodies that recognize buried epitopes are protective. Antibody-mediated immunity to WRATat 1 trypanosomes is not associated with any particular subclass of antibody. The IgM, IgG1, IgG2a, IgG2b, IgG3, and IgA subclasses each contain examples of protective monoclonal antibodies.

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