Enhancement of Sia-lb1 antigenicity by sulphur-containing substituents at C-5 of free N-acetylneuraminic acid.
The Sia-lb1 epitope, recognized by anti-Sia-lb1 cold agglutinins, is unique since it is represented by the alpha-N-acetylneuraminic acid (alpha NeuNAc) monosaccharide. Chemical modifications of the chain at C-5 of alpha NeuNAc have shown that the natural 2-carbon and the artificial 3-carbon chains are optimal for anti-Sia-lb1 binding. Sia-lb1 antigenicity of alpha NeuNAc could be tenfold enhanced by replacement of the carbonyl oxygen by sulphur. The structural requirements of the Sia-lb1 epitope for optimal antibody binding were identified.
Roelcke
D
D
Institut für Immunologie, Heidelberg, Germany.
Leo
A
A
Brossmer
R
R
D000373:Agglutinins / Q000276:immunology*; D019943:Amino Acid Substitution / Q000276:immunology*; D000603:Amino Acids, Sulfur / Q000276:immunology*; D001666:Binding Sites, Antibody; D003450:Cryoglobulins; D000939:Epitopes / Q000276:immunology; D006801:Humans; D007519:Isoantigens / Q000276:immunology*; D019158:N-Acetylneuraminic Acid / Q000276:immunology*; D013329:Structure-Activity Relationship
D000373:Agglutinins; D000603:Amino Acids, Sulfur; D003450:Cryoglobulins; D000939:Epitopes; D007519:Isoantigens; C029443:cold agglutinins; D019158:N-Acetylneuraminic Acid