Processing, polymorphism, and biological significance of P190, a major surface antigen of the erythrocytic forms of Plasmodium falciparum.
A detailed analysis of P190, a major surface associated protein of Plasmodium falciparum erythrocytic stages has been undertaken. We have demonstrated that this protein is recognised by two monoclonal antibodies, one of which recognises a constant feature (2.2) and one a variable feature (7.3). Cell free protein synthesis demonstrates that the variable 7.3 epitope is encoded in the structural gene for P190. The 7.3 epitope is only present on late trophozoites and schizonts whilst the 2.2 epitope is present on all erythrocytic stages. Labelling of synchronised cultures demonstrates that P190 is made only from 30 h onwards, (i.e. by trophozoites and schizonts). By pulse chase analysis we show that P190 undergoes processing and is lost at release/re-invasion, correlating with a lack of 7.3 immunofluorescence reactivity on rings. Sera from Nigeria recognise P190 from a Thai isolate of malaria. They also react with purified P190 in a micro-ELISA assay. A model for the role of P190 in re-invasion is presented, and the possible clinical significance of this protein is discussed.
D000818:Animals; D000954:Antigens, Surface / Q000235:genetics / Q000276:immunology*; D000939:Epitopes / Q000235:genetics; D004912:Erythrocytes / Q000276:immunology / Q000469:parasitology; D006801:Humans; D008288:Malaria / Q000097:blood / Q000276:immunology* / Q000469:parasitology; D010963:Plasmodium falciparum / Q000276:immunology*; D011110:Polymorphism, Genetic
D000954:Antigens, Surface; D000939:Epitopes