The Surface Protein SdrF Mediates Staphylococcus epidermidis Adherence to Keratin.

Trivedi, Sheetal;Uhlemann, Anne-Catrin;Herman, Philippe;Sullivan, Sean B;Lowy, Franklin D;et.al.
(2017) The Journal of Infectious Diseases — Vol. 215, p. 1846-1854 (2017)

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Authors
  • Trivedi, Sheetal
    Author
  • Uhlemann, Anne-Catrin
    Author
  • Herman, PhilippeUCLouvain
    Author
  • Sullivan, Sean B
    Author
  • Author
  • Lowy, Franklin D
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Abstract
Staphylococcus epidermidis, a major component of skin flora, is an opportunist, often causing prosthetic device infections. A family of structurally related proteins mediates staphylococcal attachment to host tissues, contributing to the success of S. epidermidis as a pathogen. We examined the ability of the surface protein SdrF to adhere to keratin, a major molecule expressed on the skin surface. A heterologous Lactococcus lactis expression system was used to express SdrF and its ligand-binding domains. Adherence to keratin types 1 and 10, human foreskin keratinocytes, and nasal epithelial cells was examined. SdrF bound human keratins 1 and 10 and adhered to keratinocytes and epithelial cells. Binding involved both the A and B domains. Anti-SdrF antibodies reduced adherence of S. epidermidis to keratin and keratinocytes. RNA interference reduced keratin synthesis in keratinocytes and, as a result, SdrF adherence. Direct force measurements using atomic force microscopy showed that SdrF mediates bacterial adhesion to keratin 10 through strong and weak bonds involving the A and B regions; strong adhesion was primarily mediated by the A region. These studies demonstrate that SdrF mediates adherence to human keratin and suggest that SdrF may facilitate S. epidermidis colonization of the skin.
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Citations

Trivedi, S., Uhlemann, A.-C., Herman, P., Sullivan, S. B., Sowash, M. G., Flores, E. Y., Khan, S. D., Dufrêne, Y., & Lowy, F. D. (2017). The Surface Protein SdrF Mediates Staphylococcus epidermidis Adherence to Keratin. The Journal of Infectious Diseases, 215, 1846-1854. https://doi.org/10.1093/infdis/jix213 (Original work published 2017)