DELINEATION AND COMPARISON OF GANGLIOSIDE-BINDING EPITOPES FOR THE TOXINS OF VIBRIO-CHOLERAE, ESCHERICHIA-COLI, AND CLOSTRIDIUM-TETANI - EVIDENCE FOR OVERLAPPING EPITOPES
DELINEATION AND COMPARISON OF GANGLIOSIDE-BINDING EPITOPES FOR THE TOXINS OF VIBRIO-CHOLERAE, ESCHERICHIA-COLI, AND CLOSTRIDIUM-TETANI - EVIDENCE FOR OVERLAPPING EPITOPES
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DOI：
10.1073/pnas.91.25.11859
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发表时间：
1994-12-06
影响因子：
11.1
通讯作者：
KARLSSON, KA
中科院分区：
文献类型：
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作者：
ANGSTROM, J;TENEBERG, S;KARLSSON, KA
已经使用微量滴定孔测定法对主要属于神经节系列的各种糖脂与从霍乱弧菌、大肠杆菌和破伤风梭菌分离的毒素进行了结合研究。通过使用所发现的结合偏好以及从各种配体的分子建模获得的最小能量构象，已经定义了毒素的天然受体糖脂上的结合表位。霍乱毒素和不耐热大肠杆菌毒素的结合偏好非常相似，神经节苷脂 GM1 是最有效的配体。破伤风毒素与 G1b 系列神经节苷脂强烈结合，其中 GT1b 是最有效的配体。研究发现，霍乱毒素和不耐热毒素GM1上的结合表位与破伤风毒素GQ1b上的表位有很大程度的重叠。
Binding studies of various glycolipids, mainly belonging to the ganglio series, to the toxins isolated from Vibrio cholerae, Escherichia coli, and Clostridium tetani have been performed, using the microtiter well assay. By using the found binding preferences in conjunction with minimum-energy conformations obtained from molecular modeling of the various ligands, binding epitopes on the natural receptor glycolipids for the toxins have been defined. The binding preferences for the cholera toxin and the heat-labile E. coli toxin are very similar, with the ganglioside GM1 being the most efficient ligand. The tetanus toxin binds strongly to gangliosides of the G1b series, with GT1b as the most efficient ligand. It is found that the binding epitope on GM1 for the cholera and heat-labile toxins to a large extent overlaps with the epitope on GQ1b for the tetanus toxin.