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Sequential binding of calcium ions to the B-repeat domain of SdrD from Staphylococcus aureus

Abstract : Biofilms of live bacteria forming on medical devices and implants contribute significantly to bacterial blood dissemination and to the spread of nosocomial infections. Cell surface SdrD protein plays a key role in the attachment of Staphylococcus aureus to the extracellular matrix (ECM) and in the formation of biofilm. SdrD binds calcium ions using its B1–B5 region bearing EF-hand Ca-binding sites, leading to conformational changes in the structure of SdrD. This alters the distance between the bacterial surface and the ECM-interacting domain of SdrD in a spring-like fashion, participating in bacterial attachment. In this study we investigated calcium binding to EF-hand sites of SdrD using isothermal titration calorimetry and determined the impact of this process on SdrD's thermodynamic stability. This allowed us to propose a model of B1–B5 reorganization upon binding of calcium and to get new insight into the molecular mechanism of SdrD's action.
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Submitted on : Tuesday, February 28, 2017 - 11:12:21 AM
Last modification on : Tuesday, December 7, 2021 - 3:33:15 PM
Long-term archiving on: : Monday, May 29, 2017 - 1:20:43 PM

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Andrei A Roman, François Devred, Vladimir M Lobatchov, Alexander A Makarov, Vincent Peyrot, et al.. Sequential binding of calcium ions to the B-repeat domain of SdrD from Staphylococcus aureus. Canadian Journal of Microbiology, 2016, 62 (2), pp.123-129. ⟨10.1139/cjm-2015-0580⟩. ⟨hal-01478554⟩

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