title: Evidence for a malarial parasite interaction site on the major transmembrane protein of the human erythrocyte.
abstract: 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.
mesh_terms: 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
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D008565:Membrane Proteins; C018059:erythroglycan; D013049:Spectrin