Sugii S
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Kanagawa, Japan.
Nihon Juigaku Zasshi. 1990 Oct;52(5):1037-42. doi: 10.1292/jvms1939.52.1037.
The binding and hemagglutinating properties of cholera toxin (CT) were studied by competitive binding assays and hemagglutination inhibition. The binding of 125I-labeled CT to neuraminidase-treated human type B erythrocytes was most effectively inhibited by ganglioside GM1 among different inhibitors used. Other mono-, di-, and polysaccharides and glycoproteins were at least 10(5) times less potent inhibitors. On the other hand, hemagglutination of neuraminidase-treated human type B erythrocytes by CT was inhibited by lactose, galactose, hog A + H, bovine salivary mucin, porcine thyroglobulin, and fetuin, whereas that was not effectively inhibited by ganglioside GM1 at the highest concentration. These findings suggest that the predominant binding substance for CT on human type B erythrocytes is ganglioside GM1 and that hemagglutination requires some additional process since the interaction of CT with ganglioside GM1 is somehow different in hemagglutination.
通过竞争性结合试验和血凝抑制试验研究了霍乱毒素（CT）的结合和血凝特性。在所用的不同抑制剂中，神经节苷脂GM1对125I标记的CT与神经氨酸酶处理的人B型红细胞的结合抑制作用最为有效。其他单糖、二糖、多糖和糖蛋白的抑制效力至少低10^5倍。另一方面，乳糖、半乳糖、猪A + H、牛唾液粘蛋白、猪甲状腺球蛋白和胎球蛋白可抑制CT对神经氨酸酶处理的人B型红细胞的血凝作用，而在最高浓度下神经节苷脂GM1对其血凝作用无有效抑制。这些发现表明，CT在人B型红细胞上的主要结合物质是神经节苷脂GM1，并且血凝需要一些额外的过程，因为CT与神经节苷脂GM1在血凝中的相互作用有所不同。
