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Four modes of adhesion are used during Helicobacter pylori binding to human mucins in the oral and gastric niches

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Author

  • Sara K. Linden
  • Claes Wickstroem
  • Gert Lindell
  • Kristen Gilshenan
  • Ingemar Carlstedt

Summary, in English

Background: Helicobacter pylori causes peptic ulcer disease and gastric cancer, and the oral cavity is likely to serve as a reservoir for this pathogen. We investigated the binding of H. pylori to the mucins covering the mucosal surfaces in the niches along the oral to gastric infection route and during gastric disease and modeled the outcome of these interactions. Materials and Methods: A panel of seven H. pylori strains with defined binding properties was used to identify binding to human mucins from saliva, gastric juice, cardia, corpus, and antrum of healthy stomachs and of stomachs affected by gastritis at pH 7.4 and 3.0 using a microtiter-based method. Results: H. pylori binding to mucins differed substantially with the anatomic site, mucin type, pH, gastritis status, and H. pylori strain all having effect on binding. Mucins from saliva and gastric juice displayed the most diverse binding patterns, involving four modes of H. pylori adhesion and the MUC5B, MUC7, and MUC5AC mucins as well as the salivary agglutinin. Binding occurred via the blood-group antigen-binding adhesin (BabA), the sialic acid-binding adhesin (SabA), a charge/low pH-dependent mechanism, and a novel saliva-binding adhesin. In the healthy gastric mucus layer only BabA and acid/charge affect binding to the mucins, whereas in gastritis, the BabA/Le(b)-dependent binding to MUC5AC remained, and SabA and low pH binding increased. Conclusions: The four H. pylori adhesion modes binding to mucins are likely to play different roles during colonization of the oral to gastric niches and during long-term infection.

Publishing year

2008

Language

English

Pages

81-93

Publication/Series

Helicobacter

Volume

13

Issue

2

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Surgery
  • Cell and Molecular Biology

Keywords

  • bacterial adhesin
  • glycosylation
  • Helicobacter pylori
  • mucin

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-4389