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Infection and Immunity, September 2001, p. 5286-5293, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5286-5293.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Borrelia burgdorferi RevA Antigen Is a Surface-Exposed Outer Membrane Protein Whose Expression Is Regulated in Response to Environmental Temperature and pH

James A. Carroll,1,* Nazira El-Hage,2 Jennifer C. Miller,2 Kelly Babb,2 and Brian Stevenson2,*

Microscopy Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840,1 and Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-02982

Received 30 March 2001/Returned for modification 15 May 2001/Accepted 29 May 2001

Borrelia burgdorferi, the causative agent of Lyme disease, produces RevA protein during the early stages of mammalian infection. B. burgdorferi apparently uses temperature as a cue to its location, producing proteins required for infection of warm-blooded animals at temperatures corresponding to host body temperature, but does not produce such virulence factors at cooler, ambient temperatures. We have observed that B. burgdorferi regulates expression of RevA in response to temperature, with the protein being synthesized by bacteria cultivated at 34°C but not by those grown at 23°C. Tissues encountered by B. burgdorferi during its infectious cycle vary in their pH values, and the level of RevA expression was also found to be dependent upon pH of the culture medium. The cellular localization of RevA was also analyzed. Borrelial inner and outer membranes were purified by isopycnic centrifugation, and membrane fractions were conclusively identified by immunoblot analysis using antibodies raised against the integral inner membrane protein MotB and outer membrane-associated Erp lipoproteins. Immunoblot analyses indicated that RevA is located in the B. burgdorferi outer membrane. These analyses also demonstrated that an earlier report (H. A. Bledsoe et al., Infect. Immun. 176:7447-7455, 1994) had misidentified such B. burgdorferi membrane fractions. RevA was further demonstrated to be exposed to the external environment, where it could facilitate interactions with host tissues.

* Corresponding authors. Mailing address for James A. Carroll: Microscopy Branch, Rocky Mountain Laboratories, NIAID, NIH, 903 South Fourth St., Hamilton, MT 59840. Phone: (406) 363-9407. Fax: (406) 363-9371. E-mail: jcarroll{at}niaid.nih.gov. Mailing address for Brian Stevenson: Department of Microbiology and Immunology, MS 415 Chandler Medical Center, University of Kentucky College of Medicine, Lexington, KY 40536-0298. Phone: (859) 257-9358. Fax: (859) 257-8994. E-mail: bstev0{at}pop.uky.edu.

Infection and Immunity, September 2001, p. 5286-5293, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5286-5293.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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