Glycoconjugate Binding of Gastric and Enterohepatic Helicobacter spp.
Författare
Summary, in English
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.
Publiceringsår
2003
Språk
Engelska
Sidor
2976-2980
Publikation/Tidskrift/Serie
Infection and Immunity
Volym
71
Issue
5
Fulltext
- Available as PDF - 182 kB
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Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Microbiology
Ämne
- Microbiology in the medical area
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1098-5522