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Infection and Immunity, July 2009, p. 2802-2812, Vol. 77, No. 7
0019-9567/09/$08.00+0     doi:10.1128/IAI.00227-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Borrelia burgdorferi RevA Antigen Binds Host Fibronectin{triangledown}

Catherine A. Brissette,* Tomasz Bykowski,§ Anne E. Cooley,{dagger} Amy Bowman, and Brian Stevenson

Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, Kentucky

Received 26 February 2009/ Returned for modification 8 April 2009/ Accepted 20 April 2009

Borrelia burgdorferi, the Lyme disease-causing spirochete, can persistently infect its vertebrate hosts for years. B. burgdorferi is often found associated with host connective tissue, where it interacts with components of the extracellular matrix, including fibronectin. Some years ago, a borrelial surface protein, named BBK32, was identified as a fibronectin-binding protein. However, B. burgdorferi BBK32 mutants are still able to bind fibronectin, indicating that the spirochete possesses additional mechanisms for adherence to fibronectin. We now demonstrate that RevA, an unrelated B. burgdorferi outer surface protein, binds mammalian fibronectin in a saturable manner. Site-directed mutagenesis studies identified the amino terminus of the RevA protein as being required for adhesion to fibronectin. RevA bound to the amino-terminal region of fibronectin. RevA binding to fibronectin was not inhibited by salt or heparin, suggesting that adhesin-ligand interactions are primarily nonionic and occur through the non-heparin-binding regions of the fibronectin amino-terminal domains. revA genes are widely distributed among Lyme disease spirochetes, and the present studies determined that all RevA alleles tested bound fibronectin. In addition, RevB, a paralogous protein found in a subset of B. burgdorferi strains, also bound fibronectin. We also confirmed that RevA is produced during mammalian infection but not during colonization of vector ticks and determined that revA transcription is controlled through a mechanism distinct from that of BBK32.

* Corresponding author. Mailing address: Department of Microbiology, Immunology and Molecular Genetics, University of Kentucky College of Medicine, Chandler Medical Center MN469, 800 Rose Street, Lexington, KY 40536-0298. Phone: (859) 257-9305. Fax: (859) 257-8994. E-mail: catherine.brissette{at}uky.edu

{triangledown} Published ahead of print on 27 April 2009.

Editor: J. B. Bliska

§ Present address: Center for Medical Education CEMED Sp. z.o.o., ul. Miedzyborska 50, 04-041 Warsaw, Poland.

{dagger} Present address: Department of Surgery, Feinberg School of Medicine, Northwestern University, Chicago, IL.

Infection and Immunity, July 2009, p. 2802-2812, Vol. 77, No. 7
0019-9567/09/$08.00+0     doi:10.1128/IAI.00227-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Verma, A., Brissette, C. A., Bowman, A., Stevenson, B. (2009). Borrelia burgdorferi BmpA Is a Laminin-Binding Protein. Infect. Immun. 77: 4940-4946 [Abstract] [Full Text]  


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