Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 25320070.
- Also identified by DOI 10.1098/rsif.2014.1040 and PMC identifier 4223928.
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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.
Medical subject headings
- Adhesins, Bacterial
- Bacterial Adhesion
- Helicobacter pylori
- Oligosaccharides