Receptor mediated endocytosis of the malarial parasite by erythrocytes
Perkins, M.E.
Progress in Clinical and Biological Research 165: 361-376
1984
ISSN/ISBN: 0361-7742 PMID: 6390454 Document Number: 236748
Plasmodium falciparum merozoites appear to interact with the major surface sialoglycoproteins, glycophorin A and glycophorin B, during entry into the human erythrocyte. Intact merozoites bind 125I-glycophorin demonstrating directly that the parasites have glycophorin binding sites. A glycophorin containing fraction crosslinked to acrylamide beads provided a probe to identify merozoite molecules with an affinity for the erythrocyte surface. A fraction of merozoites, labelled with superscript 3H-proline, and containing the membrane proteins and a fraction containing soluble proteins released by the merozoite were added to the glycophorin beads. Two proteins, of molecular weight 155 000 and 130 000, specifically bound to glycophorin. These proteins may represent the merozoite recognition site for the erythrocyte.