Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
Attempts to control human malaria by immunological means could be compromised by antigenic variability within and between different strains of malarial parasites1. A useful alternative approach might be to block parasite antigens which are important in the mechanisms of invasion of red cells. As the major human parasite Plasmodium falciparum is highly specific for human red cells, isolation of the proteins involved in the recognition of red cells by this parasite might be of particular value. Recent studies suggest that the major red cell sialoglycoproteins (SGPs), glycophorins A, B and possibly C, may carry the sites recognized by the parasite2-4. Furthermore, because certain carbohydrates present on SGPs such as N-acetylglucosamine are able to block invasion by the parasite5, they may be involved in the initial interaction between parasite and red cell. We have now identified parasite proteins which bind to SGP or N-acetylglucosamine on Sepharose 4B columns. Three proteins, of molecular weights (MWs) 140,000 (140K), 70K and 35K, seem to be specifically bound by N-acetylglucosamine.
D000117:Acetylglucosamine / Q000378:metabolism; D001665:Binding Sites; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000469:parasitology*; D006021:Glycophorins / Q000502:physiology*; D006801:Humans; D037102:Lectins; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010963:Plasmodium falciparum / Q000502:physiology*; D011485:Protein Binding; D012795:Sialoglycoproteins / Q000502:physiology*
D006021:Glycophorins; D037102:Lectins; D008565:Membrane Proteins; D012795:Sialoglycoproteins; D000117:Acetylglucosamine