From the Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, P.O. Box 440, University of Gothenburg, SE-405 30 Göteborg, Sweden and.
the Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden.
J Biol Chem. 2018 Nov 2;293(44):17248-17266. doi: 10.1074/jbc.RA118.004854. Epub 2018 Sep 19.
has a number of well-characterized carbohydrate-binding adhesins (BabA, SabA, and LabA) that promote adhesion to the gastric mucosa. In contrast, information on the glycoconjugates present in the human stomach remains unavailable. Here, we used MS and binding of carbohydrate-recognizing ligands to characterize the glycosphingolipids of three human stomachs from individuals with different blood group phenotypes (O(Rh-)P, A(Rh+)P, and A(Rh+)p), focusing on compounds recognized by We observed a high degree of structural complexity, and the composition of glycosphingolipids differed among individuals with different blood groups. The type 2 chain was the dominating core chain of the complex glycosphingolipids in the human stomach, in contrast to the complex glycosphingolipids in the human small intestine, which have mainly a type 1 core. did not bind to the O(Rh-)P stomach glycosphingolipids, whose major complex glycosphingolipids were neolactotetraosylceramide, the Le, Le, and H type 2 pentaosylceramides, and the Le hexaosylceramide. Several -binding compounds were present among the A(Rh+)P and A(Rh+)p stomach glycosphingolipids. Ligands for BabA-mediated binding of were the Le hexaosylceramide, the H type 1 pentaosylceramide, and the A type 1/ALe heptaosylceramide. Additional -binding glycosphingolipids recognized by BabA-deficient strains were lactosylceramide, lactotetraosylceramide, the x pentaosylceramide, and neolactohexaosylceramide. Our characterization of human gastric receptors required for adhesion provides a basis for the development of specific compounds that inhibit the binding of this bacterium to the human gastric mucosa.
具有许多特征明确的碳水化合物结合黏附素（BabA、SabA 和 LabA），可促进与胃黏膜的黏附。相比之下，有关人胃中存在的糖缀合物的信息仍然未知。在这里，我们使用 MS 和碳水化合物识别配体的结合来表征来自具有不同血型表型（O（Rh-）P、A（Rh+）P 和 A（Rh+）p）的三个人的胃的糖脂，重点是被 识别的化合物。我们观察到高度的结构复杂性，并且具有不同血型的个体之间的糖脂组成不同。2 型链是人类胃中复杂糖脂的主要核心链，与人类小肠中的复杂糖脂不同，后者主要具有 1 型核心。 未与 O（Rh-）P 胃糖脂结合，其主要的复杂糖脂是神经节乳糖四糖基神经酰胺、Le、Le 和 H 型 2 五糖基神经酰胺以及 Le 六糖基神经酰胺。A（Rh+）P 和 A（Rh+）p 胃糖脂中存在几种与 结合的化合物。介导与 BabA 结合的配体是 Le 六糖基神经酰胺、H 型 1 五糖基神经酰胺和 A 型 1/ALe 七糖基神经酰胺。缺乏 BabA 的菌株识别的其他与 结合的糖脂是神经节乳糖、乳糖四糖基神经酰胺、x 五糖基神经酰胺和神经节乳糖六糖基神经酰胺。我们对人胃中 黏附所需的受体的表征为开发特异性化合物提供了基础，这些化合物可抑制该细菌与人类胃黏膜的结合。
