Abstract
Helicobacter pylori 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 H. pylori 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. H. pylori did not bind to the O(Rh-)P stomach glycosphingolipids, whose major complex glycosphingolipids were neolactotetraosylceramide, the Lex, Lea, and H type 2 pentaosylceramides, and the Ley hexaosylceramide. Several H. pylori-binding compounds were present among the A(Rh+)P and A(Rh+)p stomach glycosphingolipids. Ligands for BabA-mediated binding of H. pylori were the Leb hexaosylceramide, the H type 1 pentaosylceramide, and the A type 1/ALeb heptaosylceramide. Additional H. pylori-binding glycosphingolipids recognized by BabA-deficient strains were lactosylceramide, lactotetraosylceramide, the x2 pentaosylceramide, and neolactohexaosylceramide. Our characterization of human gastric receptors required for H. pylori adhesion provides a basis for the development of specific compounds that inhibit the binding of this bacterium to the human gastric mucosa.
Highlights
Helicobacter pylori has a number of well-characterized carbohydrate-binding adhesins (BabA, SabA, and LabA) that promote adhesion to the gastric mucosa
We used MS and binding of carbohydraterecognizing 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 H. pylori
Our characterization of human gastric receptors required for H. pylori adhesion provides a basis for the development of specific compounds that inhibit the binding of this bacterium to the human gastric mucosa
Summary
Helicobacter pylori has a number of well-characterized carbohydrate-binding adhesins (BabA, SabA, and LabA) that promote adhesion to the gastric mucosa. We used MS and binding of carbohydraterecognizing 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 H. pylori. The binding of this bacterium to such diverse compounds as sialic acid-containing glycoconjugates, phosphatidylethanolamine, gangliotetraosylceramide, the Leb blood group determinant and related carbohydrate antigens, heparan sulfate, sulfatide, lactosylceramide, neolacto sequences, and lactotetraosylceramide has been documented. In contrast to the multitude of candidate H. pylori carbohydrate receptors, there are only three identified carbohydrate-binding adhesins, the blood group antigen– binding BabA2 adhesin, the sialic acid– binding SabA adhesin, and the LacdiNAc– binding LabA adhesin [5,6,7]. The adherence-associated lipoprotein A and B (AlpA/B) and the outer inflammatory protein A (OipA) are involved in H. pylori adhesion (10 –12)
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