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Glycoconjugate Binding of Gastric and Enterohepatic Helicobacter spp.

Hynes, Sean LU ; Teneberg, Susann; Roche, Niamh LU and Wadström, Torkel LU (2003) In Infection and Immunity 71(5). p.2976-2980
Abstract
Helicobacter pylori is able to utilize several lectin-like, protein-carbohydrate interactions for binding to mucins, cell surfaces, and extracellular matrix proteins. As determined by hemagglutination assays and binding of radiolabeled bacteria to glycosphingolipids on thin-layer chromatograms, strains of gastric helicobacters and enterohepatic helicobacters, including Helicobacter canis, Helicobacter hepaticus, and Helicobacter bilis, also demonstrated evidence for the presence of lectin-hemagglutinin adhesins. In addition, in H. hepaticus and H. bilis, binding may be sialic acid dependent. The presence or absence and differences in the levels of activity of lectin adhesins may reflect the species' ecological niche.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Infection and Immunity
volume
71
issue
5
pages
2976 - 2980
publisher
American Society for Microbiology
external identifiers
  • wos:000182501500085
  • pmid:12704182
  • scopus:0242500339
ISSN
1098-5522
DOI
language
English
LU publication?
yes
id
2f8ad851-de3b-4f2e-82ab-3b723ed59593 (old id 113275)
date added to LUP
2007-07-10 07:04:11
date last changed
2018-05-29 11:31:13
@article{2f8ad851-de3b-4f2e-82ab-3b723ed59593,
  abstract     = {Helicobacter pylori is able to utilize several lectin-like, protein-carbohydrate interactions for binding to mucins, cell surfaces, and extracellular matrix proteins. As determined by hemagglutination assays and binding of radiolabeled bacteria to glycosphingolipids on thin-layer chromatograms, strains of gastric helicobacters and enterohepatic helicobacters, including Helicobacter canis, Helicobacter hepaticus, and Helicobacter bilis, also demonstrated evidence for the presence of lectin-hemagglutinin adhesins. In addition, in H. hepaticus and H. bilis, binding may be sialic acid dependent. The presence or absence and differences in the levels of activity of lectin adhesins may reflect the species' ecological niche.},
  author       = {Hynes, Sean and Teneberg, Susann and Roche, Niamh and Wadström, Torkel},
  issn         = {1098-5522},
  language     = {eng},
  number       = {5},
  pages        = {2976--2980},
  publisher    = {American Society for Microbiology},
  series       = {Infection and Immunity},
  title        = {Glycoconjugate Binding of Gastric and Enterohepatic Helicobacter spp.},
  url          = {http://dx.doi.org/},
  volume       = {71},
  year         = {2003},
}