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Measurements of the binding force between the Helicobacter pylori adhesin BabA and the Lewis b blood group antigen using optical tweezers

Björnham, O; Fällman, E; Axner, O; Ohlsson, Jörgen LU ; Nilsson, Ulf LU ; Borén, T and Schedin, S (2005) In Journal of Biomedical Optics 10(4). p.044024-044032
Abstract
Helicobacter pylori is a world-wide spread bacterium that causes persistent infections and chronic inflammations that can develop into gastritis and peptic ulcer disease. It expresses several adhesin proteins on its surface that bind to specific receptors in the gastric epithelium. The most well-known adhesin is BabA, which has previously been shown to bind specifically to the fucosylated blood group antigen Lewis b (Leb). The adhesion forces between BabA and the Leb antigen are investigated in this work and assessed by means of optical tweezers. A model system for in situ measurements of the interaction forces between individual bacteria and beads coated with Leb is developed. It is found that the de-adhesion force in this model system,... (More)
Helicobacter pylori is a world-wide spread bacterium that causes persistent infections and chronic inflammations that can develop into gastritis and peptic ulcer disease. It expresses several adhesin proteins on its surface that bind to specific receptors in the gastric epithelium. The most well-known adhesin is BabA, which has previously been shown to bind specifically to the fucosylated blood group antigen Lewis b (Leb). The adhesion forces between BabA and the Leb antigen are investigated in this work and assessed by means of optical tweezers. A model system for in situ measurements of the interaction forces between individual bacteria and beads coated with Leb is developed. It is found that the de-adhesion force in this model system, measured with a loading rate of ~100 pN/s, ranges from 20 to 200 pN. The de-adhesion force appears predominantly as multiples of an elementary force, which is determined to 25±1.5 pN and identified as the unbinding force of an individual BabA-Leb binding. It is concluded that adhesion in general is mediated by a small number of bindings (most often 1 to 4) despite that the contact surface between the bacterium and the bead encompassed significantly more binding sites. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Biomedical Optics
volume
10
issue
4
pages
044024 - 044032
publisher
Published by SPIE--the International Society for Optical Engineering in cooperation with International Biomedical Optics Society
external identifiers
  • wos:000232799200033
  • scopus:32844475874
ISSN
1083-3668
DOI
10.1117/1.1989227
language
English
LU publication?
yes
id
dd9c7d3b-661b-4406-9734-b095cdea8851 (old id 158678)
date added to LUP
2007-07-10 09:22:24
date last changed
2017-03-26 03:43:23
@article{dd9c7d3b-661b-4406-9734-b095cdea8851,
  abstract     = {Helicobacter pylori is a world-wide spread bacterium that causes persistent infections and chronic inflammations that can develop into gastritis and peptic ulcer disease. It expresses several adhesin proteins on its surface that bind to specific receptors in the gastric epithelium. The most well-known adhesin is BabA, which has previously been shown to bind specifically to the fucosylated blood group antigen Lewis b (Leb). The adhesion forces between BabA and the Leb antigen are investigated in this work and assessed by means of optical tweezers. A model system for in situ measurements of the interaction forces between individual bacteria and beads coated with Leb is developed. It is found that the de-adhesion force in this model system, measured with a loading rate of ~100 pN/s, ranges from 20 to 200 pN. The de-adhesion force appears predominantly as multiples of an elementary force, which is determined to 25±1.5 pN and identified as the unbinding force of an individual BabA-Leb binding. It is concluded that adhesion in general is mediated by a small number of bindings (most often 1 to 4) despite that the contact surface between the bacterium and the bead encompassed significantly more binding sites.},
  author       = {Björnham, O and Fällman, E and Axner, O and Ohlsson, Jörgen and Nilsson, Ulf and Borén, T and Schedin, S},
  issn         = {1083-3668},
  language     = {eng},
  number       = {4},
  pages        = {044024--044032},
  publisher    = {Published by SPIE--the International Society for Optical Engineering in cooperation with International Biomedical Optics Society},
  series       = {Journal of Biomedical Optics},
  title        = {Measurements of the binding force between the Helicobacter pylori adhesin BabA and the Lewis b blood group antigen using optical tweezers},
  url          = {http://dx.doi.org/10.1117/1.1989227},
  volume       = {10},
  year         = {2005},
}