Open Access
1 July 2005 Measurements of the binding force between the Helicobacter pylori adhesin BabA and the Lewis b blood group antigen using optical tweezers
Oscar Björnham, Erik G. Fällman, Ove Axner, Jörgen Ohlsson, Ulf J. Nilsson, Thomas Borén, Staffan S. Schedin
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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.
©(2005) Society of Photo-Optical Instrumentation Engineers (SPIE)
Oscar Björnham, Erik G. Fällman, Ove Axner, Jörgen Ohlsson, Ulf J. Nilsson, Thomas Borén, and Staffan S. Schedin "Measurements of the binding force between the Helicobacter pylori adhesin BabA and the Lewis b blood group antigen using optical tweezers," Journal of Biomedical Optics 10(4), 044024 (1 July 2005). https://doi.org/10.1117/1.1989227
Published: 1 July 2005
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CITATIONS
Cited by 24 scholarly publications and 1 patent.
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KEYWORDS
Bacteria

Optical tweezers

Calibration

Receptors

Blood

Microscopes

Proteins

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