Forces driving the attachment of staphylococcus epidermidis to fibrinogen-coated surfaces
(2013) Langmuir : the A C S journal of surfaces and colloids — Vol. 29, n° 42, p. 13018-13022 (2013)
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- Cell surface proteins of bacteria play essential roles in mediating the attachment of pathogens to host tissues and, therefore, represent key targets for anti-adhesion therapy. In the opportunistic pathogen Staphylococcus epidermidis, the adhesion protein SdrG mediates attachment of bacteria to the blood plasma protein fibrinogen (Fg) through a binding mechanism that is not yet fully understood. We report the direct measurement of the forces driving the adhesion of S. epidermidis to Fg-coated substrates using single-cell force spectroscopy. We found that the S. epidermidis-Fg adhesion force is of ∼150 pN magnitude and that the adhesion strength and adhesion probability strongly increase with the interaction time, suggesting that the adhesion process involves time-dependent conformational changes. Control experiments with mutant bacteria lacking SdrG and substrates coated with the Fg β6-20 peptide, instead of the full Fg protein, demonstrate that these force signatures originate from the rupture of specific bonds between SdrG and its peptide ligand. Collectively, our results are consistent with a dynamic, multi-step ligand-binding mechanism called "dock, lock, and latch". © 2013 American Chemical Society.
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Herman, P., El Kirat, S., Beaussart, A., Geoghegan, J. A., Vanzieleghem, T., Foster, T. J., Hols, P., Mahillon, J., & Dufrêne, Y. (2013). Forces driving the attachment of staphylococcus epidermidis to fibrinogen-coated surfaces. Langmuir : the A C S journal of surfaces and colloids, 29(42), 13018-13022. https://doi.org/10.1021/la4029172 (Original work published 2013)