Evidence for a malarial parasite interaction site on the major transmembrane protein of the human erythrocyte.
Soluble oligosaccharides derived from the surface of human erythrocytes were tested for their ability to competitively inhibit invasion of erythrocytes by Plasmodium falciparum, a malarial parasite. Invasion was most effectively inhibited by erythroglycan, a carbohydrate component of the band 3 transmembrane protein. The lactosamine chains of erythroglycan contributed much of the inhibitory activity. This indication of a primary parasite interaction site on band 3 supports a role for this protein in mediating the radical alterations of the erythrocyte cytoskeleton that accompany invasion.
D001457:Anion Exchange Protein 1, Erythrocyte / Q000502:physiology*; D004705:Endocytosis; D004910:Erythrocyte Membrane / Q000469:parasitology*; D006801:Humans; D008288:Malaria / Q000503:physiopathology; D008565:Membrane Proteins / Q000502:physiology; D010963:Plasmodium falciparum / Q000502:physiology*; D013049:Spectrin / Q000502:physiology
D001457:Anion Exchange Protein 1, Erythrocyte; D008565:Membrane Proteins; C018059:erythroglycan; D013049:Spectrin