Roelcke D, Leo A, Brossmer R
Institut für Immunologie, Heidelberg, Germany.
Beitr Infusionsther Transfusionsmed. 1997;34:215-9.
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.
被抗Sia-lb1冷凝集素识别的Sia-lb1表位是独特的，因为它由α-N-乙酰神经氨酸（α-NeuNAc）单糖代表。α-NeuNAc C-5位链的化学修饰表明，天然的2-碳链和人工的3-碳链对于抗Sia-lb1结合是最佳的。用硫取代羰基氧可使α-NeuNAc的Sia-lb1抗原性增强10倍。确定了Sia-lb1表位与最佳抗体结合的结构要求。
