Surface proteins of Plasmodium falciparum merozoites binding to the erythrocyte receptor, glycophorin.

Abstract

Invasion of erythrocytes by the malarial parasite is a receptor-mediated process. P. falciparum merozoites recognize and bind to erythrocyte surface sialoglycoproteins, glycophorins A and B, and the glycophorins bind to saturable sites on the merozoite surface. The purpose of the present work was to identify a receptor or ligand molecule on the merozoite surface that mediates binding to the erythrocyte. A fraction containing the sialoglycoproteins was coupled to an acrylamide matrix and incubated with metabolically labeled merozoites. A merozoite protein of 155 kD that labeled prominently with [3H]glycine bound to glycophorin. A minor protein of 130 kD also bound. Both proteins are rich in proline and glycine, poor in methionine, and may be related. The proteins are also stable to heating to 100 degrees C for 10 min. Immunoelectron microscopy demonstrated that the 155 kD and 130 kD proteins are located on the merozoite surface coat. The antibodies significantly inhibited merozoite invasion into erythrocytes and also binding of the proteins to the glycophorin-matrix. The specific binding of the 155-kD and 130-kD proteins to the erythrocyte receptor and the demonstration that they are located on the merozoite surface suggest they could be receptor proteins that mediate binding of the merozoite to the erythrocyte surface.