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Glycophorin both in solution and inserted into liposomes blocks invasion of erythrocytes by the malaria parasite Plasmodium falciparum. Furthermore, one sugar, N-acetyl-D-glucosamine (GlcNAc), completely blocks invasion of the erythrocyte by this parasite. GlcNAc coupled to bovine serum albumin to prevent the sugar entering infected erythrocytes was at least 100,000 times more effective than GlcNAc alone. Bovine serum albumin coupled to lactose or bovine serum albumin alone had no effect on invasion. These results suggest that the binding of P. falciparum to erythrocytes is lectin-like and is determined by carbohydrates on glycophorin.

Original publication




Journal article


Proc Natl Acad Sci U S A

Publication Date





1018 - 1022


Animals, Binding, Competitive, Carbohydrate Sequence, Erythrocyte Membrane, Erythrocytes, Glycoproteins, Humans, Monosaccharides, Plasmodium falciparum, Receptors, Mitogen, Structure-Activity Relationship