Enhancement of Sia-lb1 antigenicity by sulphur-containing substituents at C-5 of free N-acetylneuraminic acid

• Verfasst von: Roelcke, Dieter [VerfasserIn]
• Verfasst von: Leo, Albrecht [VerfasserIn]
• Verfasst von: Brossmer, Reinhard [VerfasserIn]
• Titel: Enhancement of Sia-lb1 antigenicity by sulphur-containing substituents at C-5 of free N-acetylneuraminic acid
• Verf.angabe: D. Roelcke, A. Leo, R. Brossmer
• Jahr: 1997
• Umfang: 5 S.
• Titel Quelle: Enthalten in: Beiträge zur Infusionstherapie und Transfusionsmedizin
• Ort Quelle: Basel [u.a.] : Karger, 1994
• Jahr Quelle: 1997
• Band/Heft Quelle: 34(1997), Seite 215-219
• Sprache: eng
• Sach-SW: Agglutinins
• Sach-SW: Amino Acid Substitution
• Sach-SW: Amino Acids, Sulfur
• Sach-SW: Binding Sites, Antibody
• Sach-SW: Cryoglobulins
• Sach-SW: Epitopes
• Sach-SW: Humans
• Sach-SW: Isoantigens
• Sach-SW: N-Acetylneuraminic Acid
• Sach-SW: Structure-Activity Relationship
• K10plus-PPN: 1750554623

Abstract

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.