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Infect Immun, June 1998, p. 2666-2673, Vol. 66, No. 6
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

A Fibrinogen-Binding Protein of Staphylococcus epidermidis

Martin Nilsson,1 Lars Frykberg,1 Jan-Ingmar Flock,2 Lei Pei,2 Martin Lindberg,1 and Bengt Guss1,*

Department of Microbiology, Swedish University of Agricultural Sciences, S-750 07 Uppsala,1 and Department of Immunology, Microbiology, Pathology and Infectious Diseases, Karolinska Institute, Huddinge University Hospital, S-141 86 Huddinge,2 Sweden

Received 14 October 1997/Returned for modification 26 November 1997/Accepted 16 March 1998

The present study reports on fibrinogen (Fg) binding of Staphylococcus epidermidis. Adhesion of different S. epidermidis strains to immobilized Fg was found to vary significantly between different strains, and the component responsible was found to be proteinaceous in nature. To further characterize the Fg-binding activity, a shotgun phage display library covering the S. epidermidis chromosome was constructed. By affinity selection (panning) against immobilized Fg, a phagemid clone, pSEFG1, was isolated, which harbors an insert with an open reading frame of ~1.7 kilobases. Results from binding and inhibition experiments demonstrated that the insert of pSEFG1 encodes a specific Fg-binding protein. Furthermore, affinity-purified protein encoded by pSEFG1 completely inhibited adhesion of S. epidermidis to immobilized Fg. By additional cloning and DNA sequence analyses, the complete gene, termed fbe, was found to consist of an open reading frame of 3,276 nucleotides encoding a protein, called Fbe, with a deduced molecular mass of ~119 kDa. With a second phage display library made from another clinical isolate of S. epidermidis, it was possible to localize the Fg-binding region to a 331-amino-acid-long fragment. PCR analysis showed that the fbe gene was found in 40 of 43 clinical isolates of S. epidermidis. The overall organization of Fbe resembles those of other extracellular surface proteins of staphylococci and streptococci. Sequence comparisons with earlier known proteins revealed that this protein is related to an Fg-binding protein of Staphylococcus aureus called clumping factor.

* Corresponding author. Mailing address: Department of Microbiology, Swedish University of Agricultural Sciences, Box 7025, S-750 07 Uppsala, Sweden. Phone: 46 18 673205. Fax: 46 18 673392. E-mail: Bengt.Guss{at}mikrob.slu.se.

Infect Immun, June 1998, p. 2666-2673, Vol. 66, No. 6
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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