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

Linden, Sara K.; Wickstroem, Claes; Lindell, Gert LU ; Gilshenan, Kristen and Carlstedt, Ingemar LU (2008) In Helicobacter 13(2). p.81-93
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
bacterial adhesin, glycosylation, Helicobacter pylori, mucin
in
Helicobacter
volume
13
issue
2
pages
81 - 93
publisher
Wiley-Blackwell
external identifiers
  • wos:000253758900002
  • scopus:40449090246
ISSN
1083-4389
DOI
10.1111/j.1523-5378.2008.00587.x
language
English
LU publication?
yes
id
6a06d4cc-2628-4656-97c0-01ead160194a (old id 1193288)
date added to LUP
2008-09-05 14:16:59
date last changed
2017-07-30 03:51:08
@article{6a06d4cc-2628-4656-97c0-01ead160194a,
  abstract     = {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.},
  author       = {Linden, Sara K. and Wickstroem, Claes and Lindell, Gert and Gilshenan, Kristen and Carlstedt, Ingemar},
  issn         = {1083-4389},
  keyword      = {bacterial adhesin,glycosylation,Helicobacter pylori,mucin},
  language     = {eng},
  number       = {2},
  pages        = {81--93},
  publisher    = {Wiley-Blackwell},
  series       = {Helicobacter},
  title        = {Four modes of adhesion are used during Helicobacter pylori binding to human mucins in the oral and gastric niches},
  url          = {http://dx.doi.org/10.1111/j.1523-5378.2008.00587.x},
  volume       = {13},
  year         = {2008},
}