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

Paula Parreira | Zendy; Quanming Shi | Zendy; Ana Magalhães | Zendy; Celso A. Reis | Zendy; Jeanna Bugaytsova | Zendy; Thomas Borén | Zendy; Deborah Leckband | Zendy; M. Cristina L. Martins | Zendy

Open Access

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

Author(s) -

Paula Parreira,

Quanming Shi,

Ana Magalhães,

Celso A. Reis,

Jeanna Bugaytsova,

Thomas Borén,

Deborah Leckband,

M. Cristina L. Martins

Publication year - 2014

Publication title -

journal of the royal society interface

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.655

H-Index - 139

eISSN - 1742-5689

pISSN - 1742-5662

DOI - 10.1098/rsif.2014.1040

Subject(s) - bacterial adhesin , helicobacter pylori , atomic force microscopy , ligand (biochemistry) , chemistry , microscopy , antigen , group (periodic table) , blood group antigens , crystallography , biology , microbiology and biotechnology , materials science , immunology , nanotechnology , escherichia coli , genetics , biochemistry , physics , receptor , optics , gene , organic chemistry

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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