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J. Biol. Chem., Vol. 277, Issue 45, 43017-43023, November 8, 2002
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From the The opportunistic human pathogen
Staphylococcus epidermidis is the major cause of nosocomial
biomaterial infections. S. epidermidis has the ability to
attach to indwelling materials coated with extracellular matrix
proteins such as fibrinogen, fibronectin, vitronectin, and collagen. To
identify the proteins necessary for S. epidermidis
attachment to collagen, we screened an expression library using
digoxigenin-labeled collagen as well as two monoclonal antibodies
generated against the Staphylococcus aureus
collagen-adhesin, Cna, as probes. These monoclonal antibodies recognize
collagen binding epitopes on the surface of S. aureus and
S. epidermidis cells. Using this approach, we identified
GehD, the extracellular lipase originally found in S. epidermidis 9, as a collagen-binding protein. Despite the
monoclonal antibody cross-reactivity, the GehD amino acid sequence and
predicted structure are radically different from those of Cna. The
mature GehD circular dichroism spectra differs from that of Cna but
strongly resembles that of a mammalian cell-surface collagen binding
receptor, known as the
Is the GehD Lipase from Staphylococcus epidermidis a
Collagen Binding Adhesin?*
,
Institute of Biosciences and Technology, The
Texas A & M University System Health Science Center, Houston, Texas
77030, § Department of Biochemistry, University of Pavia,
Viale Taramelli 3/B, I-27100 Pavia, Italy, and ¶ Division of
Microbiology, School of Biochemistry and Molecular Biology, University
of Leeds, Leeds LS2 9JT, United Kingdom
1 integrin I domain, suggesting
that they have similar secondary structures. The GehD protein is
translated as a preproenzyme, secreted, and post-translationally
processed into mature lipase. GehD does not have the conserved
LPXTG C-terminal motif present in cell wall-anchored
proteins, but it can be detected in lysostaphin cell wall extracts. A
recombinant version of mature GehD binds to collagens type I, II, and
IV adsorbed onto microtiter plates in a dose-dependent
saturable manner. Recombinant, mature GehD protein and anti-GehD
antibodies can inhibit the attachment of S. epidermidis to
immobilized collagen. These results provide evidence that GehD may be a
bi-functional molecule, acting not only as a lipase but also as a cell
surface-associated collagen adhesin.
*
This work was supported by National Institutes of Health
Grant AR44415 (to M. H.) and postdoctoral fellowship award AI 10629 (to M. G. B.). This study was also supported by grants from
Fondazione Cariplo, 2002 and Ricerca Finalizzata Ministero della
Sanità, 2001 (to P. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Institute of
Biosciences and Technology, The Texas A & M University System Health Science Center, 2121 W. Holcombe Blvd., Houston, TX 77030. Tel.: 713-677-7551l; Fax: 713-677-7576; E-mail: mhook@ibt.tamu.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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