Sugii S, Tsuji T
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Japan.
FEMS Microbiol Lett. 1990 Jan 1;54(1-3):45-50. doi: 10.1016/0378-1097(90)90256-p.
The binding and hemagglutinating activities of the B subunit(s) of the heat-labile enterotoxin (LTh-B) isolated from human enterotoxigenic Escherichia coli were investigated. The binding of 125I-labeled LTh-B to neuraminidase-treated human type B erythrocytes was most effectively inhibited by ganglioside GM1. A number of mono-, di- and polysaccharides, as well as several glycoproteins were at least 500 times less potent inhibitors. However, hemagglutination was effectively inhibited by galactose, melibiose and hog A + H but not by ganglioside GM1. Preincubation of the LTh-B with ganglioside GM1 gave much stronger hemagglutination than LTh-B alone. These results suggest that the predominant binding substance for LTh-B on neuraminidase-treated human type B erythrocytes is ganglioside GM1, but indicate that the interaction of LTh-B with ganglioside GM1 is different in hemagglutination.
对从人产肠毒素大肠杆菌中分离出的不耐热肠毒素（LTh-B）的B亚基的结合和血凝活性进行了研究。神经氨酸酶处理过的人B型红细胞对125I标记的LTh-B的结合作用，最有效的抑制剂是神经节苷脂GM1。许多单糖、双糖和多糖以及几种糖蛋白作为抑制剂的效力至少低500倍。然而，半乳糖、蜜二糖和猪A + H可有效抑制血凝，而神经节苷脂GM1则不能。LTh-B与神经节苷脂GM1预孵育后的血凝作用比单独的LTh-B强得多。这些结果表明，神经氨酸酶处理过的人B型红细胞上LTh-B的主要结合物质是神经节苷脂GM1，但表明LTh-B与神经节苷脂GM1在血凝方面的相互作用有所不同。
