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J. Biol. Chem., Vol. 279, Issue 49, 50710-50716, December 3, 2004

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Identification and Characterization of the C3 Binding Domain of the Staphylococcus aureus Extracellular Fibrinogen-binding Protein (Efb)^*

Lawrence Y. L. Lee, Xiaowen Liang, Magnus Höök, and Eric L. Brown

From the Center for Extracellular Matrix Biology, Texas A&M University System Health Science Center, Albert B. Alkek Institute of Biosciences and Technology, Houston, Texas, 77030-7552

The secreted Staphylococcus aureus extracellular fibrinogen-binding protein (Efb) is a virulence factor that binds to both the complement component C3b and fibrinogen. Our laboratory previously reported that by binding to C3b, Efb inhibited complement activation and blocked opsonophagocytosis. We have now located the Efb binding domain in C3b to the C3d fragment and determined a disassociation constant (K_d) of 0.24 µM for the Efb-C3d binding using intrinsic fluorescence quenching assays. Using truncated, recombinant forms of Efb, we also demonstrate that the C3b binding region of Efb is located within the C terminus, in contrast to the fibrinogen binding domains that are located at the N-terminal end of the protein. Enzyme-linked immunosorbent assay-type binding assays demonstrated that recombinant Efb could bind to both C3b and fibrinogen simultaneously, forming a trimolecular complex and that the C-terminal region of Efb could inhibit complement activity in vitro. In addition, secondary structure analysis using circular dichroism spectroscopy revealed that the C-terminal, C3b binding region of Efb is composed primarily of -helices, suggesting that this domain of Efb represents a novel type of C3b-binding protein.

Received for publication, July 28, 2004 , and in revised form, August 16, 2004.

^* 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.

Present address and to whom correspondence and reprint requests should be addressed: Wyle Laboratories Bioastronautics Team, Human Adaptation and Countermeasures, Wyle/HAC/W1, 1290 Hercules Dr., 120, Office 408, Houston, TX 77058. Tel.: 281-212-1421; Fax: 281-212-1316; E-mail: ebrown{at}wylehou.com.

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