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

• Type: Article in International Scientific Journal
• Date: 2014

Authors

Parreira, P (Author) Other; Shi, Q (Author) Other; Magalhaes, A (Author) Other; Celso Reis (Author) ICBAS; Bugaytsova, J (Author) Other; Boren, T (Author) Other; Leckband, D (Author) Other; Martins, MCL (Author) Other

Journal

Title: Journal of the Royal Society Interface

Vol. 11

Pages: 20141040-20141040

ISSN: 1742-5689

Publisher: The Royal Society

Indexing

ISI Web of Knowledge - 10 Citations

Scopus - 12 Citations

Other information

Authenticus ID: P-009-XFP

DOI: 10.1098/rsif.2014.1040

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7