Characterization of epitopes on a variant surface glycoprotein from Trypanosoma congolense by six monoclonal antibodies.
Monoclonal antibodies were isolated from mice immunized with variant surface glycoprotein of Trypanosoma congolense. Five out of the six monoclonals were able to detect epitopes at the cell surface in an indirect immunofluorescence analysis. One antibody did not react. Using protein-A-containing bacterial adsorbent all monoclonal antibodies precipitate glycosylated as well as non-glycosylated variant surface glycoprotein. Carbohydrate chains therefore do not appear to be part of the immunodeterminant structure recognized by the various monoclonal antibodies. Interaction of the monoclonal antibodies with protein fragments obtained by partial proteolysis with V8 protease from Staphylococcus aureus or papain allows the classification of the antibodies into three groups with different epitope specificity.
D000818:Animals; D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes / Q000032:analysis*; D005455:Fluorescent Antibody Technique; D008970:Molecular Weight; D014348:Trypanosoma congolense / Q000254:growth & development / Q000276:immunology*; D014643:Variant Surface Glycoproteins, Trypanosoma / Q000276:immunology* / Q000302:isolation & purification
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D014643:Variant Surface Glycoproteins, Trypanosoma