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Open Access Research article

Surface proteins that promote adherence of Staphylococcus aureus to human desquamated nasal epithelial cells

Rebecca M Corrigan, Helen Miajlovic and Timothy J Foster*

Author Affiliations

Microbiology Department, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Ireland

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BMC Microbiology 2009, 9:22  doi:10.1186/1471-2180-9-22

Published: 30 January 2009

Abstract

Background

The natural habitat of Staphylococcus aureus is the moist squamous epithelium in the anterior nares. About 20% of the human population carry S. aureus permanently in their noses and another 60% of individuals are intermittent carriers. The ability of S. aureus to colonize the nasal epithelium is in part due to expression of surface proteins clumping factor B (ClfB) and the iron-regulated surface determinant A (IsdA), which promote adhesion to desquamated epithelial cells present in the anterior part of the nasal vestibule. S. aureus strain Newman defective in IsdA and ClfB exhibited reduced but not completely defective adherence to squamous cells in indicating that other cell surface components might also contribute.

Results

Surface proteins IsdA, ClfB, and the serine-aspartic acid repeat proteins SdrC, SdrD and SdrE were investigated to determine their contribution to the adherence of S. aureus to desquamated nasal epithelial cells. This was achieved by expression of ClfB, IsdA, SdrC, SdrD and SdrE on the surface of the surrogate Gram-positive host Lactococcus lactis and by isolating mutants of S. aureus Newman defective in one or more factor. The level of adherence of strains to squamous cells isolated from the nares of volunteers was measured. Results consistently showed that ClfB, IsdA, SdrC and SdrD each contributed to the ability of S. aureus to adhere to squamous cells. A mutant lacking all four proteins was completely defective in adherence.

Conclusion

The ability of S. aureus Newman to adhere to desquamated nasal epithelial cells is multifactorial and involves SdrD and SdrC as well as ClfB and IsdA.