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Infection and Immunity, November 2005, p. 7398-7405, Vol. 73, No. 11
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.11.7398-7405.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Borrelia burgdorferi Regulates Expression of Complement Regulator-Acquiring Surface Protein 1 during the Mammal-Tick Infection Cycle

Kate von Lackum,1 Jennifer C. Miller,1 Tomasz Bykowski,1 Sean P. Riley,1 Michael E. Woodman,1 Volker Brade,2 Peter Kraiczy,2 Brian Stevenson,1* and Reinhard Wallich3

Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298,1 Institute of Medical Microbiology, University Hospital of Frankfurt, Frankfurt, Germany, D-60596,2 Department of Immunology, University of Heidelberg, Heidelberg, Germany, D-691203

Received 19 May 2005/ Returned for modification 27 June 2005/ Accepted 15 August 2005

During the natural mammal-tick infection cycle, the Lyme disease spirochete Borrelia burgdorferi comes into contact with components of the alternative complement pathway. B. burgdorferi, like many other human pathogens, has evolved the immune evasion strategy of binding two host-derived fluid-phase regulators of complement, factor H and factor H-like protein 1 (FHL-1). The borrelial complement regulator-acquiring surface protein 1 (CRASP-1) is a surface-exposed lipoprotein that binds both factor H and FHL-1. Analysis of CRASP-1 expression during the mammal-tick infectious cycle indicated that B. burgdorferi expresses this protein during mammalian infection, supporting the hypothesized role for CRASP-1 in immune evasion. However, CRASP-1 synthesis was repressed in bacteria during colonization of vector ticks. Analysis of cultured bacteria indicated that CRASP-1 is differentially expressed in response to changes in pH. Comparisons of CRASP-1 expression patterns with those of other infection-associated B. burgdorferi proteins, including the OspC, OspA, and Erp proteins, indicated that each protein is regulated through a unique mechanism.

* Corresponding author. Mailing address: Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, MS417 Chandler Medical Center, 800 Rose Street, Lexington, KY 40536-0298. Phone: (859) 257-9358. Fax: (859) 257-8994. E-mail: bstev0{at}uky.edu.

Editor: D. L. Burns

Infection and Immunity, November 2005, p. 7398-7405, Vol. 73, No. 11
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.11.7398-7405.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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