The malaria merozoite surface: a 140,000 m.w. protein antigenically unrelated to other surface components on Plasmodium knowlesi merozoites.

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Abstract
We previously identified three proteins on the surface of merozoites (140,000, 105,000 and 75,000 m.w.). To determine if 140,000 m.w. protein was related to other surface proteins, we immunized mice with liposomes containing merozoite proteins from the 140,000 m.w. region of the polyacrylamide gel. The immune sera reacted with the surface of viable merozoites and acetone-fixed schizonts by immunofluorescence. The sera immunoprecipitated only the 140,000 m.w. protein from surface-labeled merozoites. We demonstrated that monoclonal antibody 13C11 immunoprecipitated a 250,000 m.w. protein from metabolically labeled schizonts and bound to the merozoite surface. This monoclonal antibody immunoprecipitated the 75,000 and lower m.w. proteins from surface-labeled merozoites but did not bring down the 140,000 m.w. protein. Because the mouse immune sera did not immunoprecipitate the 250,000 m.w. protein from metabolically labeled schizonts or proteins other than the 140,000 m.w. protein from surface-labeled merozoites, we conclude that the 140,000 m.w. protein is unrelated to other merozoite surface antigens identified to date. The mouse immune sera against the 140,000 m.w. protein on the merozoite surface did not immunoprecipitate a 140,000 m.w. protein from metabolically labeled schizonts. Instead, the major protein immunoprecipitated had a m.w. of 144,000. By analogy to the 250,000 m.w. protein and its cleavage products, we propose that the 140,000 m.w. protein on the merozoite surface is a cleavage product of the higher m.w. protein.