Helicobacter pylori SabA binding gangliosides of human stomach

Virulence
John BenktanderSusann Teneberg

Abstract

Adhesion of Helicobacter pylori to the gastric mucosa is a prerequisite for the pathogenesis of H. pylori related diseases. In this study, we investigated the ganglioside composition of human stomach as the target for attachment mediated by H. pylori SabA (sialic acid binding adhesin). Acid glycosphingolipids were isolated from human stomach and separated into subfractions, which were characterized by mass spectrometry and by binding of antibodies, bacteria, and Solanum tuberosum lectin. H. pylori SabA binding gangliosides were characterized as Neu5Acα3-neolactohexaosylceramide and Neu5Acα3-neolactooctaosylceramide, while the other acid human stomach glycosphingolipids characterized (sulfatide and the gangliosides GM3, GD3, GM1, Neu5Acα3-neolactotetraosylceramide, GD1a and GD1b) were not recognized by the bacteria. Defining H. pylori binding glycosphingolipids of the human gastric mucosa will be useful to specifically target this microbe-host interaction for therapeutic intervention.

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Citations

Jun 20, 2020·European Journal of Clinical Microbiology & Infectious Diseases : Official Publication of the European Society of Clinical Microbiology·Chenjing XuShunfu Xu
Sep 21, 2018·The Journal of Biological Chemistry·Chunsheng JinSusann Teneberg
Dec 24, 2019·Frontiers in Cell and Developmental Biology·Johannes M F G AertsR G Boot
Nov 11, 2020·Scientific Reports·Licínia SantosSusann Teneberg
May 25, 2021·Frontiers in Molecular Biosciences·Rita MatosCelso A Reis
Jul 3, 2021·Biomolecules·Patrycja BurzyńskaEwa Jaśkiewicz
Dec 31, 2021·Helicobacter·Rita MatosFátima Gärtner

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Methods Mentioned

BETA
scrapings
glycosylation

Software Mentioned

Glycoworkbench
Xcalibur

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