Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand

J R Soc Interface. 2014 Dec 6;11(101):20141040. doi: 10.1098/rsif.2014.1040.

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.

Keywords: Helicobacter pylori; Lewis b; adhesion force; atomic force microscopy; blood group antigen-binding adhesin; self-assembled monolayers.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adhesins, Bacterial / chemistry
  • Adhesins, Bacterial / metabolism*
  • Bacterial Adhesion / physiology*
  • Gastric Mucosa / chemistry
  • Gastric Mucosa / metabolism
  • Gastric Mucosa / microbiology
  • Helicobacter pylori / metabolism*
  • Helicobacter pylori / ultrastructure
  • Humans
  • Lewis Blood Group Antigens
  • Microscopy, Atomic Force
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism*

Substances

  • 3-aminopropyl fucopyranosyl-1-2-galactopyranosyl-1-3-(fucopyranosyl-1-4)-2-acetamido-2-deoxyglucopyranosyl-1-3-galactopyranosyl-1-4-glucopyranoside
  • Adhesins, Bacterial
  • BabA protein, Helicobacter pylori
  • Lewis Blood Group Antigens
  • Oligosaccharides