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Helicobacter suis binding to carbohydrates on human and porcine gastric mucins and glycolipids occurs via two modes

Journal article
Authors Médea Padra
Barbara Adamczyk
John Benktander
B. Flahou
Emma C Skoog
János T Padra
A. Smet
Chunsheng Jin
R. Ducatelle
Tore Samuelsson
F. Haesebrouck
Niclas G. Karlsson
Susann Teneberg
Sara K. Lindén
Published in Virulence
Volume 9
Issue 1
Pages 898-918
ISSN 2150-5594
Publication year 2018
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 898-918
Language en
Keywords Helicobacter suis, Helicobacter pylori, bacterial adhesion, host-pathogen interactions, mucin, liquid chromatography/mass spectrometry, structural diversity, mucus, glycoproteins, surface epithelium, pylori infection, gene-expression, colonic mucins, pigs, adhesin, identification
Subject categories Infectious Medicine, Microbiology in the medical area


Helicobacter suis colonizes the stomach of most pigs and is the most prevalent non-Helicobacter pylori Helicobacter species found in the human stomach. In the human host, H. suis contributes to the development of chronic gastritis, peptic ulcer disease and MALT lymphoma, whereas in pigs it is associated with gastritis, decreased growth and ulcers. Here, we demonstrate that the level of H. pylori and H. suis binding to human and pig gastric mucins varies between individuals with species dependent specificity. The binding optimum of H. pylori is at neutral pH whereas that of H. suis has an acidic pH optimum, and the mucins that H. pylori bind to are different than those that H. suis bind to. Mass spectrometric analysis of mucin O-glycans from the porcine mucin showed that individual variation in binding is reflected by a difference in glycosylation; of 109 oligosaccharide structures identified, only 14 were present in all examined samples. H. suis binding to mucins correlated with glycans containing sulfate, sialic acid and terminal galactose. Among the glycolipids present in pig stomach, binding to lactotetraosylceramide (Gal beta 3GlcNAc beta 3Gal beta 4Glc beta 1Cer) was identified, and adhesion to Gal beta 3GlcNAc beta 3Gal beta 4Glc at both acidic and neutral pH was confirmed using other glycoconjugates. Together with that H. suis bound to DNA (used as a proxy for acidic charge), we conclude that H. suis has two binding modes: one to glycans terminating with Gal beta 3GlcNAc, and one to negatively charged structures. Identification of the glycan structures H. suis interacts with can contribute to development of therapeutic strategies alternative to antibiotics.

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