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Infection and Immunity, June 2009, p. 2408-2416, Vol. 77, No. 6
0019-9567/09/$08.00+0     doi:10.1128/IAI.01304-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Iron-Regulated Surface Determinant Protein A Mediates Adhesion of Staphylococcus aureus to Human Corneocyte Envelope Proteins{triangledown}

Simon R. Clarke,1,2,{dagger} Guillaume Andre,3,{dagger} Evelyn J. Walsh,4 Yves F. Dufrêne,3 Timothy J. Foster,4 and Simon J. Foster1*

Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, United Kingdom,1 School of Biological Sciences, University of Reading, Whiteknights, Reading, RG6 6AJ, United Kingdom,2 Unité de Chimie des Interfaces, Université Catholique de Louvain, Croix du Sud 2/18, 1348 Louvain-la-Neuve, Belgium,3 Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Ireland4

Received 24 October 2008/ Returned for modification 8 December 2008/ Accepted 12 March 2009

The ability of Staphylococcus aureus to colonize the human nares is a crucial prerequisite for disease. IsdA is a major S. aureus surface protein that is expressed during human infection and required for nasal colonization and survival on human skin. In this work, we show that IsdA binds to involucrin, loricrin, and cytokeratin K10, proteins that are present in the cornified envelope of human desquamated epithelial cells. To measure the forces and dynamics of the interaction between IsdA and loricrin (the most abundant protein of the cornified envelope), single-molecule force spectroscopy was used, demonstrating high-specificity binding. IsdA acts as a cellular adhesin to the human ligands, promoting whole-cell binding to immobilized proteins, even in the absence of other S. aureus components (as shown by heterologous expression in Lactococcus lactis). Inhibition experiments revealed the binding of the human ligands to the same IsdA region. This region was mapped to the NEAT domain of IsdA. The NEAT domain also was found to be required for S. aureus whole-cell binding to the ligands as well as to human nasal cells. Thus, IsdA is an important adhesin to human ligands, which predominate in its primary ecological niche.

* Corresponding author. Mailing address: Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, United Kingdom. Phone: 44 114 222 4411. Fax: 44 114 222 2800. E-mail: s.foster{at}sheffield.ac.uk

{triangledown} Published ahead of print on 23 March 2009.

Editor: B. A. McCormick

{dagger} These authors contributed equally to this research.

Infection and Immunity, June 2009, p. 2408-2416, Vol. 77, No. 6
0019-9567/09/$08.00+0     doi:10.1128/IAI.01304-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Macintosh, R. L., Brittan, J. L., Bhattacharya, R., Jenkinson, H. F., Derrick, J., Upton, M., Handley, P. S. (2009). The Terminal A Domain of the Fibrillar Accumulation-Associated Protein (Aap) of Staphylococcus epidermidis Mediates Adhesion to Human Corneocytes. J. Bacteriol. 191: 7007-7016 [Abstract] [Full Text]  


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