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Strain- and blood group-dependent binding of Helicobacter pylori to human gastric MUC5AC glycoforms.

Lindén, Sara LU ; Nordman, Henrik LU ; Hedenbro, Jan LU ; Hurtig, Marina; Borén, Thomas and Carlstedt, Ingemar LU (2002) In Gastroenterology 123(6). p.1923-1930
Abstract
Background & Aims: In the stomach, Helicobacter pylori is found both in the mucus layer and adhering to the gastric epithelium. The aim of this study is to characterize the binding of H. pylori to human gastric mucins. Methods:H. pylori strains that bind the Lewisb (Leb) structure (via the BabA adhesin) and/or sialylated structures, along with isogenic adhesion deletion mutants, were used to identify microbe-binding mucins. Gastric mucins from 5 healthy individuals, isolated by density-gradient centrifugation, were investigated for H. pylori binding at neutral pH using a microtiter-based technique. Results:H. pylori strains that express the BabA adhesins were shown to bind to the MUC5AC mucin in individuals expressing the Leb antigen.... (More)
Background & Aims: In the stomach, Helicobacter pylori is found both in the mucus layer and adhering to the gastric epithelium. The aim of this study is to characterize the binding of H. pylori to human gastric mucins. Methods:H. pylori strains that bind the Lewisb (Leb) structure (via the BabA adhesin) and/or sialylated structures, along with isogenic adhesion deletion mutants, were used to identify microbe-binding mucins. Gastric mucins from 5 healthy individuals, isolated by density-gradient centrifugation, were investigated for H. pylori binding at neutral pH using a microtiter-based technique. Results:H. pylori strains that express the BabA adhesins were shown to bind to the MUC5AC mucin in individuals expressing the Leb antigen. Further fractionation with an ion-exchange chromatography revealed Leb-positive MUC5AC glycoforms that differed in their receptor properties for different H. pylori strains. None of the H. pylori strains studied bound to mucins from Leb-negative individuals. However, all strains bound to low-density, nonmucin, Leb-negative material on top of the gradients. Conclusions: Binding of H. pylori to human gastric MUC5AC isolated from healthy individuals is BabA dependent and mediated by the Leb structure presented by the mucin. However, the BabA adhesins demonstrate strain-dependent preference in binding to MUC5AC glycoforms substituted with Leb, allowing for great interindividual variability in host–microbe interactions. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Gastroenterology
volume
123
issue
6
pages
1923 - 1930
publisher
W B Saunders
external identifiers
  • pmid:12454849
  • wos:000179545300023
  • scopus:0036892334
ISSN
1528-0012
DOI
10.1053/gast.2002.37076
language
English
LU publication?
yes
id
b47e80c2-0351-498d-88f5-506df1715678 (old id 110899)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12454849&dopt=Abstract
date added to LUP
2007-07-17 09:21:48
date last changed
2017-10-01 03:52:39
@article{b47e80c2-0351-498d-88f5-506df1715678,
  abstract     = {Background & Aims: In the stomach, Helicobacter pylori is found both in the mucus layer and adhering to the gastric epithelium. The aim of this study is to characterize the binding of H. pylori to human gastric mucins. Methods:H. pylori strains that bind the Lewisb (Leb) structure (via the BabA adhesin) and/or sialylated structures, along with isogenic adhesion deletion mutants, were used to identify microbe-binding mucins. Gastric mucins from 5 healthy individuals, isolated by density-gradient centrifugation, were investigated for H. pylori binding at neutral pH using a microtiter-based technique. Results:H. pylori strains that express the BabA adhesins were shown to bind to the MUC5AC mucin in individuals expressing the Leb antigen. Further fractionation with an ion-exchange chromatography revealed Leb-positive MUC5AC glycoforms that differed in their receptor properties for different H. pylori strains. None of the H. pylori strains studied bound to mucins from Leb-negative individuals. However, all strains bound to low-density, nonmucin, Leb-negative material on top of the gradients. Conclusions: Binding of H. pylori to human gastric MUC5AC isolated from healthy individuals is BabA dependent and mediated by the Leb structure presented by the mucin. However, the BabA adhesins demonstrate strain-dependent preference in binding to MUC5AC glycoforms substituted with Leb, allowing for great interindividual variability in host–microbe interactions.},
  author       = {Lindén, Sara and Nordman, Henrik and Hedenbro, Jan and Hurtig, Marina and Borén, Thomas and Carlstedt, Ingemar},
  issn         = {1528-0012},
  language     = {eng},
  number       = {6},
  pages        = {1923--1930},
  publisher    = {W B Saunders},
  series       = {Gastroenterology},
  title        = {Strain- and blood group-dependent binding of Helicobacter pylori to human gastric MUC5AC glycoforms.},
  url          = {http://dx.doi.org/10.1053/gast.2002.37076},
  volume       = {123},
  year         = {2002},
}