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Helicobacter pylori-binding nonacid glycosphingolipids in the human stomach
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics. Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, P.O. Box 440, University of Gothenburg, SE-405 30 Göteborg, Sweden.
2018 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 293, no 44, p. 17248-17266Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology, 2018. Vol. 293, no 44, p. 17248-17266
Keywords [en]
Helicobacter pylori, mass spectrometry (MS), glycolipid structure, adhesin, carbohydrate structure, ycoconjugate, virulence factor, gastric mucosa, glycosphingolipid characterization, H, pylori BabA hesin, Human gastric glycosphingolipids, microbial adhesion
National Category
Biochemistry and Molecular Biology Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-153648DOI: 10.1074/jbc.RA118.004854ISI: 000449466500024PubMedID: 30232154OAI: oai:DiVA.org:umu-153648DiVA, id: diva2:1266040
Available from: 2018-11-27 Created: 2018-11-27 Last updated: 2018-11-27Bibliographically approved

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Boren, ThomasSandberg, Susanne

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