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J Biol Chem, Vol. 275, Issue 18, 13863-13871, May 5, 2000
From the Center for Extracellular Matrix Biology and the Department
of Biochemistry and Biophysics, Institute of Biosciences and
Technology, Texas A&M University System Health Science Center,
Houston, Texas 77030-3303
Staphylococcus aureus is an important
pathogen capable of causing a wide spectrum of diseases in humans and
animals. This bacterium expresses a variety of virulence factors that
participate in the process of infection. These include MSCRAMMs
(microbial surface components
recognizing adhesive matrix
molecules) that mediate the adherence of the bacteria to
host extracellular matrix components, such as collagen, fibronectin
(Fn), and fibrinogen (Fg). Two Fn-binding MSCRAMMs, FnbpA and FnbpB,
have been previously identified. The Fn binding activity has been
localized to the ~40-amino acid residue D repeats in the C-terminal
part of these proteins. However, no biological activity has yet been
attributed to the N-terminal A regions of these proteins. These regions
exhibit substantial amino acid sequence identity to the A regions of
other staphylococcal MSCRAMMs, including ClfA, ClfB, and SdrG (Fbe), all of which bind Fg. This raises the question of whether the Fn-binding MSCRAMMs can also bind specifically to Fg. In this report,
we show that a recombinant form of the A region of FnbpA does
specifically recognize Fg. We localize the binding site in Fg for
recombinant FnbpA to the
The Fibronectin-binding MSCRAMM FnbpA of
Staphylococcus aureus Is a Bifunctional Protein
That Also Binds to Fibrinogen*
,
-chain, in particular to the C-terminal
residues of this polypeptide, the site also recognized by ClfA. In
addition, we demonstrate that recombinant FnbpA can compete with ClfA
for binding to both immobilized and soluble Fg. By the use of surface
plasmon resonance spectroscopy and fluorescence polarization, we
determine the dissociation equilibrium constant for the interaction of
recombinant FnbpA with intact immobilized Fg and with a synthetic
C-terminal -chain peptide, respectively. Finally, by overexpressing
FnbpA in a mutant strain of S. aureus that lacks the
expression of both ClfA and ClfB, we show that native FnbpA can mediate
the interaction of S. aureus with soluble Fg.
*
This work was supported by National Institutes of Health
Grant AI20624 (to M. H.).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: Center for
Extracellular Matrix Biology and Dept. of Biochemistry and Biophysics, Inst. of Biosciences and Technology, Texas A&M University System Health
Science Center, 2121 W. Holcombe Blvd., Houston, TX 77030-3303. Tel.:
713-677-7541; Fax: 713-677-7576; E-mail: ewann@ibt.tamu.edu.
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