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首页> 外文期刊>Infection and immunity >Comparison of the Tissue Receptors for Vibrio cholerae and Escherichia coli Enterotoxins by Means of Gangliosides and Natural Cholera Toxoid
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Comparison of the Tissue Receptors for Vibrio cholerae and Escherichia coli Enterotoxins by Means of Gangliosides and Natural Cholera Toxoid

机译：用神经节苷脂和天然霍乱类毒素比较霍乱弧菌和大肠杆菌肠毒素的组织受体

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The in vitro binding properties of enterotoxins of Vibrio cholerae and Escherichia coli to different pure gangliosides and related neutral glycosphin-golipids were analyzed with a sorbent assay utilizing plastic tubes to which the glycolipid substances had been coupled. It was found that the cholera toxin bound to GM1 ganglioside better than to the other tested substances GM3, GM3-NGN, GM2, GD1a, GD1b, GT, GA1, tetrahexoside-GlcNac and globoside. With this assay using GM1-coated tubes it is possible to measure cholera toxin even at concentrations below 1 ng/ml. Also enterotoxin of various E. coli strains bound to GM1, but the affinity was much less than for cholera toxin. The GM1 ganglioside, in contrast to the other glycosphingolipids, effectively inactivated cholera toxin as determined with the intradermal and the ileal loop assays; approximately equimolar concentrations of the ganglioside in relation to toxin sufficed. Also, the skin and ileal loop activities of E. coli enterotoxins could be inhibited by GM1; however, several orders more of the ganglioside were required for such inhibition than for inactivation of the cholera toxin, and the differences between GM1 and the other substances were less pronounced for E. coli toxins. Preincubation of rabbit ileal loops with choleragenoid, a natural toxoid of V. cholerae which has binding properties to the GM1 ganglioside similar to cholera toxin, made the loops resistant to subsequently added enterotoxin of V. cholerae. The responsiveness to enterotoxin of E. coli was not reduced by this toxoid. A likely interpretation of these data is that the GM1 ganglioside constitutes or at least contains the structure of functional tissue receptors for the cholera toxin, whereas the weak binding to GM1 by E. coli enterotoxins is probably a pathogenetically insignificant reflection of structural similarities between these toxins and cholera toxin. Consequently, the cholera toxoid by occupying functional intestinal GM1 receptors for the cholera toxin could inhibit the ileal response to this toxin, but not the response to E. coli enterotoxin since the intestinal receptors for the latter toxin are not affected by the cholera toxoid.
机译：利用塑料管进行的吸附剂吸附法分析了霍乱弧菌和大肠杆菌的肠毒素与不同纯神经节苷脂和相关中性糖鞘磷脂的体外结合特性。物质已经耦合。结果发现，霍乱毒素与神经节苷脂G M1 的结合要优于其他受试物质G M3 ，G M3 -NGN，G < sub> M2 ，G D1a ，G D1b ，G T ，G A1 ，四己糖苷- GlcNac和globoside。通过使用涂有G M1 的试管进行这种测定，即使浓度低于1 ng / ml，也可以测量霍乱毒素。还包括各种 E的肠毒素。大肠埃希菌与G M1 结合，但亲和力远小于霍乱毒素。与其他糖鞘脂相比，G M1 神经节苷脂可以有效地灭活霍乱毒素，这是通过皮内和回肠loop分析确定的。相对于毒素而言，神经节苷脂的浓度大约为等摩尔。此外， E的皮肤和回肠loop活动。 G M1 可抑制大肠毒素。然而，这种抑制作用所需的神经节苷脂比霍乱毒素的灭活要多几个数量级，而G M1 与其他物质之间的差异对于 E则不那么明显。大肠杆菌毒素。兔回肠loop与霍乱类毒素（ V的天然类毒素）的预培养。与霍乱毒素相似，与G M1 神经节苷脂具有结合特性的霍乱，使环对随后添加的 V肠毒素具有抗性。霍乱。对 E肠毒素的反应。这种类毒素不会降低大肠杆菌。这些数据的可能解释是，G M1 神经节苷脂构成或至少包含霍乱毒素的功能性组织受体结构，而G M1 E。大肠杆菌肠毒素可能是这些毒素与霍乱毒素之间结构相似性的病原学上微不足道的反映。因此，霍乱类毒素通过占据霍乱毒素的功能性肠道G M1 受体可以抑制回肠对这种毒素的应答，但不能抑制对 E的应答。肠毒素，因为后者毒素的肠受体不受霍乱类毒素影响。

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