Purification and characterization of culture-derived exoantigens of Plasmodium falciparum.
An 83 kDa glycoprotein and a 100 kDa glycoprotein have been purified from the supernatant fluid of in vitro cultures of Plasmodium falciparum by conventional cation-exchange liquid chromatography, size exclusion high performance liquid chromatography, and anion-exchange high performance liquid chromatography. Both proteins exist as dimers in the native state and have been identified as parasite antigens by Western immunoblotting and by their specific reactivity in the indirect enzyme-linked immunosorbent assay. The N-terminal amino acid sequence of these two proteins has been determined and they are at least 90% homologous. The use of monospecific rabbit antisera raised against the individual pure proteins confirm their cross-reactivity. We postulate that the 83 kDa protein is a specific processing product of the larger 100 kDa protein. The presence of these proteins in the culture supernatant suggests they could both be derived from the merozoite surface coat and are potential protective antigens.
D000595:Amino Acid Sequence; D000818:Animals; D000953:Antigens, Protozoan / Q000276:immunology / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D005260:Female; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D008565:Membrane Proteins / Q000276:immunology / Q000302:isolation & purification; D008970:Molecular Weight; D010963:Plasmodium falciparum / Q000276:immunology*
D000953:Antigens, Protozoan; D006023:Glycoproteins; D008565:Membrane Proteins