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

P. Parreira, Q. Shi, A. Magalhaes, C. A. Reis, J. Bugaytsova, T. Borén, D. Leckband, M. C.L. Martins

Research output: Contribution to journalArticle

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 (Leb), 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 Leb 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.

Original languageEnglish (US)
Article number20141040
JournalJournal of the Royal Society Interface
Volume11
Issue number101
DOIs
StatePublished - Dec 6 2014

Keywords

  • Adhesion force
  • Atomic force microscopy
  • Blood group antigen-binding adhesin
  • Helicobacter pylori
  • Lewis b
  • Self-assembled monolayers

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Bioengineering
  • Biomaterials
  • Biochemistry
  • Biomedical Engineering

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