Antigenic cross reactivity between p195 and a distinct protein of 100 kDa in Plasmodium falciparum.
A monoclonal antibody raised against merozoites of Plasmodium falciparum clone T9/96 was shown to react with an extremely strain specific epitope on a 195 kDa protein synthesized only by late trophozoites and schizonts. This protein was shown to exhibit all of the characteristics attributed to the molecule known variously as merozoite surface protein precursor, polymorphic schizont antigen and p195. The monoclonal antibody also identified a cross-reactive epitope on a distinct protein of 100 kDa in ring stage parasites which was shown to be synthesized throughout the asexual cycle and was not a processing product of p195. One-dimensional peptide mapping studies suggested that these two proteins share a degree of common sequence or structure.
D000818:Animals; D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan / Q000032:analysis / Q000276:immunology*; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000032:analysis / Q000276:immunology; D008970:Molecular Weight; D010449:Peptide Mapping; D010963:Plasmodium falciparum / Q000276:immunology*; D011506:Proteins / Q000032:analysis / Q000276:immunology*; D011863:Radioimmunoassay
D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan; D000939:Epitopes; D011506:Proteins