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, Deborah E 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

Fingerprint

Atomic Force Microscopy
Antigens
Blood Group Antigens
Helicobacter pylori
Atomic force microscopy
Blood
Ligands
Bacterial Adhesion
Self assembled monolayers
Gastric Mucosa
Adhesives
Polysaccharides
Rupture
Spectrum Analysis
Adhesion
Spectroscopy
Population

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

Cite this

Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand. / Parreira, P.; Shi, Q.; Magalhaes, A.; Reis, C. A.; Bugaytsova, J.; Borén, T.; Leckband, Deborah E; Martins, M. C.L.

In: Journal of the Royal Society Interface, Vol. 11, No. 101, 20141040, 06.12.2014.

Research output: Contribution to journalArticle

Parreira, P. ; Shi, Q. ; Magalhaes, A. ; Reis, C. A. ; Bugaytsova, J. ; Borén, T. ; Leckband, Deborah E ; Martins, M. C.L. / Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand. In: Journal of the Royal Society Interface. 2014 ; Vol. 11, No. 101.
@article{4ac860f50c21415eaddff111410981a9,
title = "Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand",
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.",
keywords = "Adhesion force, Atomic force microscopy, Blood group antigen-binding adhesin, Helicobacter pylori, Lewis b, Self-assembled monolayers",
author = "P. Parreira and Q. Shi and A. Magalhaes and Reis, {C. A.} and J. Bugaytsova and T. Bor{\'e}n and Leckband, {Deborah E} and Martins, {M. C.L.}",
year = "2014",
month = "12",
day = "6",
doi = "10.1098/rsif.2014.1040",
language = "English (US)",
volume = "11",
journal = "Journal of the Royal Society Interface",
issn = "1742-5689",
publisher = "Royal Society of London",
number = "101",

}

TY - JOUR

T1 - Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand

AU - Parreira, P.

AU - Shi, Q.

AU - Magalhaes, A.

AU - Reis, C. A.

AU - Bugaytsova, J.

AU - Borén, T.

AU - Leckband, Deborah E

AU - Martins, M. C.L.

PY - 2014/12/6

Y1 - 2014/12/6

N2 - 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.

AB - 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.

KW - Adhesion force

KW - Atomic force microscopy

KW - Blood group antigen-binding adhesin

KW - Helicobacter pylori

KW - Lewis b

KW - Self-assembled monolayers

UR - http://www.scopus.com/inward/record.url?scp=84921665680&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84921665680&partnerID=8YFLogxK

U2 - 10.1098/rsif.2014.1040

DO - 10.1098/rsif.2014.1040

M3 - Article

C2 - 25320070

AN - SCOPUS:84921665680

VL - 11

JO - Journal of the Royal Society Interface

JF - Journal of the Royal Society Interface

SN - 1742-5689

IS - 101

M1 - 20141040

ER -