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J. Biol. Chem., Vol. 279, Issue 37, 38433-38440, September 10, 2004

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The N-terminal A Domain of Fibronectin-binding Proteins A and B Promotes Adhesion of Staphylococcus aureus to Elastin^*

Fiona M. Roche, Robert Downer, Fiona Keane, Pietro Speziale¶, Pyong Woo Park||, and Timothy J. Foster**

From the Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Ireland, the ^¶Department of Biochemistry, University of Pavia, Pavia, Italy, and the ^||Department of Medicine, Baylor College of Medicine, Houston, Texas 77030

The ability of Staphylococcus aureus to adhere to components of the extracellular matrix is an important mechanism for colonization of host tissues during infection. We have previously shown that S. aureus binds elastin, a major component of the extracellular matrix. The integral membrane protein, elastin-binding protein (EbpS), binds soluble elastin peptides and tropoelastin via its surface-exposed N-terminal domain. In this study, we demonstrate that some strains of S. aureus adhere strongly to immobilized human elastin and that this interaction is independent of EbpS but instead is mediated by the fibronectin-binding proteins, FnBPA and FnBPB. Our results show that EbpS mutant cells adhere to elastin-coated plates, whereas the cells negative for FnBPA and FnBPB do not adhere to the plates. Furthermore, only wild-type cells from the exponential phase of growth adhered when FnBPs were expressed maximally. We show that adherence to elastin promoted by FnBPA was not affected by soluble fibronectin, suggesting that the elastin binding domain is distinct from the fibronectin binding regions. Recombinant FnBPA_37–544 (rFnBPA_37–544) protein corresponding to the A region of FnBPA and anti-FnBPA_37–544 antibodies inhibited FnBPA-mediated bacterial adherence to immobilized elastin. Finally, recombinant A domain proteins, rFnBPA_37–544 and rFnBPB_37–540, bound immobilized elastin dose-dependently and saturably. This interaction was inhibited by soluble elastin peptides, suggesting a specific receptor-ligand interaction.

Received for publication, February 26, 2004 , and in revised form, July 2, 2004.

^* This work was supported by grants from Enterprise Ireland, the Health Research Board of Ireland, and Inhibitex Inc. 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.

Both authors contributed equally to this work.

^** To whom correspondence should be addressed. Tel.: 353-1-6082014; Fax: 353-1-6799294; E-mail: tfoster{at}tcd.ie.

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