-binding nonacid glycosphingolipids in the human stomach.

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.