Miller-Podraza H, Larsson T, Nilsson J, Teneberg S, Matrosovich M, Johansson L
Department of Medical Biochemistry, Göteborg University, Sweden.
Acta Biochim Pol. 1998;45(2):439-49.
Receptor-active gangliosides with affinity for Helicobacter pylori and influenza virus were chemically modified and analyzed by negative ion fast atom bombardment mass spectrometry (FAB MS) or electron ionization mass spectrometry (EI MS) after permethylation. Derivatizations included mild periodate oxidation of the sialic acid glycerol tail or conversion of the carboxyl group to primary alcohol or amides. The modified gangliosides were then tested for binding affinity using thin-layer plates overlaid with labeled microbes or microbe-derived proteins. Mild periodate oxidation, which shortens sialic acid tail without destruction of sugar cores, abolished or drastically reduced binding of H. pylori and avian influenza virus to sialyl-3-paragloboside (S-3-PG). The same effect was observed in the case of binding of the human influenza virus to receptor-active gangliosides of human leukocytes. Conversion of S-3-PG or leukocyte gangliosides to primary alcohols or amides also abolished the binding. However, mild periodate oxidation had no effect on binding of NAP (neutrophil-activating protein of H. pylori) to the active ganglioside.
对具有幽门螺杆菌和流感病毒亲和力的受体活性神经节苷脂进行化学修饰，并在全甲基化后通过负离子快原子轰击质谱（FAB MS）或电子电离质谱（EI MS）进行分析。衍生化包括对唾液酸甘油尾部进行温和的高碘酸盐氧化，或将羧基转化为伯醇或酰胺。然后使用覆盖有标记微生物或微生物衍生蛋白的薄层板测试修饰后的神经节苷脂的结合亲和力。温和的高碘酸盐氧化可缩短唾液酸尾部而不破坏糖核心，消除或显著降低幽门螺杆菌和禽流感病毒与唾液酸-3-副球蛋白（S-3-PG）的结合。在人类流感病毒与人白细胞的受体活性神经节苷脂结合的情况下也观察到了相同效果。将S-3-PG或白细胞神经节苷脂转化为伯醇或酰胺也消除了结合。然而，温和的高碘酸盐氧化对幽门螺杆菌的中性粒细胞活化蛋白（NAP）与活性神经节苷脂的结合没有影响。
