Glycoconjugate Binding of Gastric and Enterohepatic Helicobacter spp.
(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:
https://lup.lub.lu.se/record/113275
- author
- Hynes, Sean LU ; Teneberg, Susann ; Roche, Niamh LU and Wadström, Torkel LU
- organization
- publishing date
- 2003
- 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
- 10.1128/IAI.71.5.2976-2980.2003
- language
- English
- LU publication?
- yes
- id
- 2f8ad851-de3b-4f2e-82ab-3b723ed59593 (old id 113275)
- date added to LUP
- 2016-04-01 11:55:29
- date last changed
- 2022-04-13 03:19:43
@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 = {{https://lup.lub.lu.se/search/files/2704455/623735.pdf}}, doi = {{10.1128/IAI.71.5.2976-2980.2003}}, volume = {{71}}, year = {{2003}}, }