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Journal for Biophysical Chemistry

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Atomic force microscopy and surface plasmon resonance investigation of fibronectin interactions with group B streptococci

Biointerphases volume 2, pages 64–72 (2007)Cite this article

Abstract

The interactions of fibronectin (Fn) with group B streptococci (GBS) were investigated using the atomic force microscope (AFM) and surface plasmon resonance (SPR) biosensing. Submonolayer amounts of Fn were immobilized onto the AFM tip by two different methods, using either a sulfosuccinimidyl-4-(N-maleimidomethyl) cycholhexane-1-carboxylate (SMCC) linker or a pyridyldithio poly(ethylene glycol) succinimidylpropionate (NHS-PEG-PDP) linker. Each step of both immobilization methods was characterized using x-ray photoelectron spectroscopy. Time-of-flight secondary ion mass spectrometry experiments indicated both methods produced Fn immobilized in a similar conformation. AFM force-distance curves from live GBS plated onto polystyrene exhibited several types of interactions between the Fn functionalized AFM tip and the surface of capsule-deficient GBS (no interactions, interactions with the cell wall, Fn unfolding, large specific unbinding events, and small specific unbinding events). From analysis of the force-distance curves that exhibited only a single specific unbinding event, the work of adhesion and rupture force for the SMCC immobilized Fn tips (11 131 pN nm and 213 pN) were larger than the corresponding values for the NHS-PEG-PDP immobilized Fn tips (8115 pN nm and 189 pN). The unbinding event occurred at distances approximately 100 nm further from the surface with the NHS-PEG-PDP immobilized Fn tip compared to SMCC immobilized Fn tip. The SPR experiments of soluble Fn with adsorbed serine protease C5a peptidase (Scp), the surface protein on GBS that binds Fn, showed that both low (millimolar) and high binding (nanomolar) affinity interactions were present. However, the low binding affinity interactions dominated the adsorption process and, with increasing Fn solution concentration, the amount of Scp bound to Fn via the high binding affinity interaction decreased. These data confirm that Scp binds only to adsorbed Fn at the Fn concentrations typically present in blood plasma.

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Authors and Affiliations

  1. National ESCA and Surface Analysis Center for Biomedical Problems and Department of Chemical Engineering, University of Washington, Box 351750, 98195-1750, Seattle, Washington

    James R. Hull & Jared J. Shannon

  2. Division of Infectious Disease and Department of Pediatrics, Children’s Hospital and Regional Medical Center and University of Washington, 4800 Sand Point Way NE, 98105, Seattle, Washington

    Glen S. Tamura

  3. National ESCA and Surface Analysis Center for Biomedical Problems, Department of Chemical Engineering, and Department of Bioengineering, University of Washington, Box 351750, 98195-1750, Seattle, Washington

    David G. Castner

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  1. James R. Hull
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  2. Jared J. Shannon
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  3. Glen S. Tamura
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  4. David G. Castner
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Correspondence to David G. Castner.

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Hull, J.R., Shannon, J.J., Tamura, G.S. et al. Atomic force microscopy and surface plasmon resonance investigation of fibronectin interactions with group B streptococci. Biointerphases 2, 64–72 (2007). https://doi.org/10.1116/1.2738854

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  • DOI: https://doi.org/10.1116/1.2738854