Change search
ReferencesLink to record
Permanent link

Direct link
Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Show others and affiliations
2013 (English)In: Acta biomaterialia, ISSN 1878-7568, Vol. 9, no 11, 8885-8893 p.Article in journal (Refereed) Published
Abstract [en]

Helicobacter pylori colonizes the gastric mucosa of half of the worlds population and persistent infection is related with an increase in the risk of gastric cancer. Adhesion of H. pylori to the gastric epithelium, which is essential for infection, is mediated by bacterial adhesin proteins that recognize specific glycan structures (Gly-R) expressed in the gastric mucosa. The blood group antigen binding adhesin (BabA) recognizes difucosylated antigens such as Lewis B (Le(b)), while the sialic acid binding adhesin (SabA) recognizes sialylated glycoproteins and glycolipids, such as sialyl-Lewis x (sLe(x)). This work aimed to investigate whether these Gly-Rs (Le(b) and sLe(x)) can attract and specifically bind H. pylori after immobilization on synthetic surfaces (self-assembled monolayers (SAMs) of alkanethiols on gold). Functional bacterial adhesion assays for (Gly-R)-SAMs were performed using H. pylori strains with different adhesin protein profiles. The results demonstrate that H. pylori binding to surfaces occurs via interaction between its adhesins and cognate (Gly-R)-SAMs and bound H. pylori maintains its characteristic rod-shaped morphology only during conditions of specific adhesin-glycan binding. These results offer new insights into innovative strategies against H. pylori infection based on the scavenging of bacteria from the stomach using specific H. pylori chelating biomaterials.

Place, publisher, year, edition, pages
2013. Vol. 9, no 11, 8885-8893 p.
Keyword [en]
Helicobacter pylori, Functionalized nanostructured surfaces, Self-assembled monolayers, Blood group antigen binding adhesin, Sialic acid binding adhesin
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:umu:diva-82540DOI: 10.1016/j.actbio.2013.06.042PubMedID: 23831721OAI: diva2:661815
Available from: 2013-11-05 Created: 2013-11-05 Last updated: 2013-12-16Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Borén, Thomas
By organisation
Department of Medical Biochemistry and Biophysics
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 34 hits
ReferencesLink to record
Permanent link

Direct link