Affiliation:
1. Cellular Microbiology Research Group, Eastman Dental Institute for Oral Health Care Sciences, University College London, London WC1X 8LD, United Kingdom
Abstract
ABSTRACT
Staphylococcus epidermidis
has been reported to bind to a number of host cell extracellular matrix proteins, including fibronectin. Here we report the identification of a fibronectin-binding protein from
S. epidermidis
. A phage display library of
S. epidermidis
genomic DNA was constructed and panned against immobilized fibronectin. A number of phagemid clones containing overlapping inserts were identified, and one of these clones, pSE109FN, contained a 1.4-kb insert. Phage pSE109FN was found to bind to fibronectin but not to collagen, fibrinogen, laminin, or vitronectin. However, pSE109FN also bound to heparin, hyaluronate, and plasminogen, although to a lesser extent than it bound to fibronectin. Analysis of The Institute for Genomic Research
S. epidermidis
genome sequence database revealed a 1.85-kb region within a putative 30.5-kb open reading frame, to which the overlapping DNA inserts contained within the fibronectin-binding phagemids mapped. We have designated the gene encoding the fibronectin-binding domain
embp
. A recombinant protein, Embp32, which encompassed the fibronectin-binding domain of Embp, blocked the binding of
S. epidermidis
, but not the binding of
Staphylococcus aureus
, to fibronectin. In contrast, a recombinant protein, FnBPB[D1-D4], spanning the fibronectin-binding domain of the
S. aureus
fibronectin-binding protein FnBPB, blocked binding of
S. aureus
to fibronectin but had a negligible effect on the binding of
S. epidermidis
.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
133 articles.
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