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J. Biol. Chem., Vol. 279, Issue 40, 41706-41714, October 1, 2004

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BBK32, a Fibronectin Binding MSCRAMM from Borrelia burgdorferi, Contains a Disordered Region That Undergoes a Conformational Change on Ligand Binding^*

Jung Hwa Kim, Jenny Singvall, Ulrich Schwarz-Linek¶||, Barbara J. B. Johnson**, Jennifer R. Potts¶, and Magnus Höök

From the Center for Extracellular Matrix Biology, Albert B. Alkek Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, Texas 77030, ^¶Department of Biochemistry, University of Oxford, South Parks Rd., United Kingdom, and ^**Division of Vector-Borne Infectious Disease, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Fort Collins, Colorado 80522

BBK32 is a fibronectin-binding lipoprotein on Borrelia burgdorferi, the causative agent of Lyme disease. Analysis using secondary structure prediction programs suggested that BBK32 is composed of two domains, an N-terminal segment lacking well defined secondary structure and a C-terminal segment composed largely of -helices. Analysis of purified recombinant forms of the two domains by circular dichroism spectroscopy, gel permeation chromatography, and intrinsic viscosity determination were consistent with an N-terminal-extended, unstructured segment and a C-terminal globular domain in BBK32. Solid phase binding experiments suggest that the unstructured N-terminal domain binds fibronectin. Analysis of changes in circular dichroism spectra of the N-terminal segment of BBK32 upon binding of the N-terminal domain of fibronectin revealed an increase in -sheet content in the complex. Hence, BBK32, which belongs to a different family of proteins and shows no overall sequence similarity with the fibronectin binding MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) of Gram-positive bacteria, binds fibronectin by a mechanism that is reminiscent of the "tandem -zipper" previously demonstrated for the fibronectin binding of streptococcal adhesins (Schwarz-Linek, U., Werner, J. M., Pickford, A. R., Gurusiddappa, S., Kim, J. H., Pilka, E. S., Briggs, J. A., Gough, T. S., Hook, M., Campbell, I. D., and Potts, J. R. (2003) Nature 423, 177–181).

Received for publication, February 16, 2004 , and in revised form, July 27, 2004.

^* 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. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a fellowship from the Life Science Task Force at Texas A&M University.

^|| This author acknowledges the Biotechnology and Biological Sciences Research Council, Swindon, United Kingdom for financial support.

This author acknowledges the British Heart Foundation and the Wellcome Trust for financial support.

To whom correspondence should be addressed: Center for Extracellular Matrix Biology, Albert B. Alkek Institute of Biosciences and Technology, Texas A&M University System Health Science Center, 2121 W. Holcombe Blvd., Houston, TX 77030. Tel.: 713-677-7551; Fax: 713-677-7576; E-mail:mhook{at}ibt.tamu.edu.

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