Role of the carbohydrate domains of glycophorins as erythrocyte receptors for invasion by Plasmodium falciparum merozoites.
Solubilized preparations of purified glycophorins and specific domains of these molecules were assessed for their effects as inhibitors of Plasmodium falciparum invasion of human erythrocytes in vitro. The ability of newly invaded merozoites to continue developing and incorporating [3H]hypoxanthine during a 24-h period after their invasion was used as an assay for merozoite invasion. Glycophorins A, B, and C were found to be equally effective as inhibitors. Previous studies had shown N-acetylglucosamine, a sugar component of glycophorins A and C but not B, to be an effective inhibitor. Accordingly, molecular domains common to all of the glycophorins were further assessed. Sialic acid was shown to act almost as effectively as N-acetylglucosamine, presumably because of the structural similarities between these sugars. The inhibitory ability of sialic acid is considerably enhanced when presented to the parasite in a clustered form, as in an oligosaccharide. The acetyl group of these sugars does not appear to play an essential role in this inhibition. How the P. falciparum merozoite recognizes and interacts with the sugar domains of the glycophorin molecule remains to be determined.
D000818:Animals; D004910:Erythrocyte Membrane / Q000382:microbiology*; D006020:Glycopeptides / Q000494:pharmacology; D006021:Glycophorins / Q000502:physiology*; D006023:Glycoproteins / Q000097:blood / Q000494:pharmacology; D006736:Horses; D006801:Humans; D007700:Kinetics; D010446:Peptide Fragments / Q000032:analysis; D010963:Plasmodium falciparum / Q000187:drug effects / Q000254:growth & development / Q000472:pathogenicity*; D012756:Sheep; D012795:Sialoglycoproteins / Q000502:physiology*; D013045:Species Specificity; D014357:Trypsin
D006020:Glycopeptides; D006021:Glycophorins; D006023:Glycoproteins; D010446:Peptide Fragments; D012795:Sialoglycoproteins; D014357:Trypsin