Strain- and blood group-dependent binding of Helicobacter pylori to human gastric MUC5AC glycoforms.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/110899
- author
- Lindén, Sara LU ; Nordman, Henrik LU ; Hedenbro, Jan LU ; Hurtig, Marina ; Borén, Thomas and Carlstedt, Ingemar LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Gastroenterology
- volume
- 123
- issue
- 6
- pages
- 1923 - 1930
- publisher
- Elsevier
- 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
- 2016-04-01 12:19:52
- date last changed
- 2022-03-13 08:28:41
@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 = {{Elsevier}},
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}},
doi = {{10.1053/gast.2002.37076}},
volume = {{123}},
year = {{2002}},
}