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J. Biol. Chem., Vol. 282, Issue 26, 18767-18776, June 29, 2007

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SdrF, a Staphylococcus epidermidis Surface Protein, Binds Type I Collagen^*

Carlos Arrecubieta, Mei-Ho Lee, Alistair Macey¹, Timothy J. Foster, and Franklin D. Lowy^¶2

From the Division of Infectious Diseases, Department of Medicine, and the ^¶Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, New York 10032 and the Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Ireland

Staphylococcus epidermidis is the leading cause of device-related infections. These infections require an initial colonization step in which S. epidermidis adheres to the implanted material. This process is usually mediated by specific bacterial surface proteins and host factors coating the foreign device. Some of these surface proteins belong to the serine-aspartate repeat (Sdr) family, which includes adhesins from Staphyloccus aureus and S. epidermidis. Using a heterologous expression system in Lactococcus lactis to overcome possible staphylococcal adherence redundancy we observed that one of these Sdr proteins, SdrF, mediates binding to type I collagen when present on the lactococcal cell surface. We used lactococcal recombinant strains, a protein-protein interaction assay and Western ligand blot analysis to demonstrate that this process occurs via the B domain of SdrF and both the 1 and 2 chains of type I collagen. It was also found that a single B domain repeat of S. epidermidis 9491 retains the capacity to bind to type I collagen. We demonstrated that the putative ligand binding N-terminal A domain does not bind to collagen which suggests that SdrF might be a multiligand adhesin. Antibodies directed against the B domain significantly reduce in vitro adherence of S. epidermidis to immobilized collagen.

Received for publication, November 28, 2006 , and in revised form, March 20, 2007.

^* This work was supported in part by Grant HL 077096-01 from the NHLBI, National Institutes of Health-Specialized Center for Clinically Oriented Research, by the Health Research Board (Program Grant PRO 09/2002), and the Science Foundation Ireland (to T. J. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S3 and Table S1.

¹ Present address: Dept. of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Ireland.

² To whom correspondence should be addressed: Dept. of Medicine, Columbia University, 630 W. 168th St., P&S Bldg. 9-458, New York, NY 10032. Tel.: 212-305-5787; Fax: 212-305-5794; E-mail: fl189{at}columbia.edu.

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