Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins.
The presence of terminal alpha-D-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of Plasmodium falciparum is demonstrated by the alpha-D-galactosidase sensitivity of particular parasite antigens, the use of specific glycosidases to cleave sugars from parasite glycoproteins radiolabeled with [3H]glucosamine, and the ability of Bandeirea simplicifolia lectin, which has a specificity for terminal alpha-galactosyl residues, to bind to the parasite. The carbohydrate side chains, and in particular the terminal alpha-galactosyl residues, are shown to have an important role in determining the binding of antibodies to parasite glycoproteins.
D000818:Animals; D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan / Q000276:immunology*; D001029:Aotus trivirgatus; D005690:Galactose / Q000276:immunology; D006023:Glycoproteins / Q000276:immunology*; D006026:Glycoside Hydrolases; D007106:Immune Sera; D007120:Immunochemistry; D037102:Lectins / Q000276:immunology; D037121:Plant Lectins; D010963:Plasmodium falciparum / Q000276:immunology*; D000519:alpha-Galactosidase
D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan; D006023:Glycoproteins; C045475:Griffonia simplicifolia lectins; D007106:Immune Sera; D037102:Lectins; D037121:Plant Lectins; D006026:Glycoside Hydrolases; D000519:alpha-Galactosidase; D005690:Galactose