ArticleJournal of the Royal Society, Interface2014
Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand.
Article in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- Cholesterol Functionalized Nanoparticles Are Effective against Helicobacter pylori, the Gastric Bug: A Proof-of-Concept Study.Advanced healthcare materials · 2025Article
- Probing the expression and adhesion of glycans involved in Helicobacter pylori infection.Scientific reports · 2024Article
- The biophysics of bacterial infections: Adhesion events in the light of force spectroscopy.Cell surface (Amsterdam, Netherlands) · 2021Article
- Adhesion ofFrontiers in molecular biosciences · 2021Review
- Atomic Force Microscopy Meets Biophysics, Bioengineering, Chemistry, and Materials Science.ChemSusChem · 2019Review
- Identification of novel protein domain for sialyloligosaccharide binding essential to Mycoplasma mobile gliding.FEMS microbiology letters · 2019Article
- Promising Recent Strategies with Potential Clinical Translational Value to Combat Antibacterial Resistant Surge.Medicines (Basel, Switzerland) · 2019Review
- The Interaction of the Gut Microbiota with the Mucus Barrier in Health and Disease in Human.Microorganisms · 2018Review
- Coating nanoparticles with gastric epithelial cell membrane for targeted antibiotic delivery againstAdvanced therapeutics · 2018Article
- Pathogenesis of Helicobacter pylori Infection.Helicobacter · 2015Review
- The giant adhesin SiiE of Salmonella enterica.Molecules (Basel, Switzerland) · 2015Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The strength of binding between the Helicobacter pylori blood group antigen-binding adhesin (BabA) and its cognate glycan receptor, the Lewis b blood group antigen (Le(b)), was measured by means of atomic force microscopy. High-resolution measurements of rupture forces between single receptor-ligand pairs were performed between the purified BabA and immobilized Le(b) structures on self-assembled monolayers. Dynamic force spectroscopy revealed two similar but statistically different bond populations. These findings suggest that the BabA may form different adhesive attachments to the gastric mucosa in ways that enhance the efficiency and stability of bacterial adhesion.
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