Topography of epitopes on a polymorphic schizont antigen of Plasmodium falciparum determined by the binding of monoclonal antibodies in a two-site radioimmunoassay.
The topographic distribution of common and variant epitopes on two divergent allelic forms of the 185-205K schizont glycoprotein of Plasmodium falciparum were studied by a two-site radioimmunoassay using monoclonal antibodies. Similarities in the conformation of the two molecules were apparent. On both antigens two distinct regions were mapped, each comprising of both strain-common and polymorphic epitopes. Epitopes common to the two PSAs were found to be closely associated with different variable epitopes in tertiary structure. It is suggested that this may contribute to parasite evasion of the host immune response.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000936:Antigen-Antibody Complex / Q000032:analysis; D000953:Antigens, Protozoan / Q000276:immunology*; D000939:Epitopes / Q000032:analysis*; D006023:Glycoproteins / Q000276:immunology; D046911:Macromolecular Substances; D008970:Molecular Weight; D010963:Plasmodium falciparum / Q000276:immunology*; D011110:Polymorphism, Genetic; D011863:Radioimmunoassay
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000953:Antigens, Protozoan; D000939:Epitopes; D006023:Glycoproteins; D046911:Macromolecular Substances