Ultrastrong adhesion to human skin: Calcium as a key regulator of noncovalent interactions
(2025) Science advances — Vol. 11, n° 36, p. 19 (2025)
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- Authors
Chantraine, Constance 
Gomes, Priscila S. F. C. Mathelié-Guinlet, Marion Gomes, Diego E. B.
- Abstract
- Calcium is a critical regulator of Staphylococcus aureus skin adhesion, stabilizing one of the strongest noncovalent biomolecular interactions ever recorded. Using in vitro and in silico single-molecule force spectroscopy, we demonstrate that calcium ions (Ca2+) are essential for the ultrastrong binding between the serine-aspartate repeat protein D (SdrD) adhesin and the human skin protein desmoglein-1 (DSG-1), withstanding forces exceeding 2 nanonewtons. Ca2+ ions stabilize both the SdrD complex and the mechanically robust SdrD B-domains, which exhibit unprecedented folding strength. In the context of atopic dermatitis (AD), disrupted calcium gradients amplify SdrD interactions, which could potentially intensify S. aureus virulence. Furthermore, abnormal DSG-1 distribution on AD-affected skin enhances bacterial adhesion. These findings provide crucial insights into the calcium-dependent regulation of bacterial adhesion and folding, suggesting possible therapeutic targets to combat S. aureus infections.
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Citations
Chantraine, C., Gomes, P. S. F. C., Mathelié-Guinlet, M., Gomes, D. E. B., Zheng, Z., Clowry, J., Turley, M. B., Irvine, A. D., Geoghegan, J. A., Bernardi, R. C., & Dufrêne, Y. (2025). Ultrastrong adhesion to human skin: Calcium as a key regulator of noncovalent interactions. Science advances, 11(36), 19. https://doi.org/10.1126/sciadv.adu7457 (Original work published 2025)