This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Roberts, D. M.
Right arrow Articles by Marconi, R. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Roberts, D. M.
Right arrow Articles by Marconi, R. T.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2000, p. 4222-4226, Vol. 182, No. 15
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Analysis of the Cellular Localization of Bdr Paralogs in Borrelia burgdorferi, a Causative Agent of Lyme Disease: Evidence for Functional Diversity

David M. Roberts,1 Michael Theisen,2 and Richard T. Marconi1,*

Department of Microbiology and Immunology, School of Medicine, Medical College of Virginia at Virginia Commonwealth University, Richmond, Virginia,1 and Statens Serum Institute, Copenhagen, Denmark2

Received 3 February 2000/Accepted 15 May 2000

The bdr (Borrelia direct repeat) gene family of the genus Borrelia encodes a polymorphic group of proteins that carry a central repeat motif region containing putative phosphorylation sites and a hydrophobic carboxyl-terminal domain. It has been postulated that the Bdr proteins may anchor to the inner membrane via the C-terminal domain. In this study, we used cellular fractionation methodologies, salt and detergent treatments, and immunoblot analyses to assess the association of the Bdr proteins with the cellular infrastructure in both Borrelia burgdorferi (a Lyme disease spirochete) and B. turicatae (a relapsing fever spirochete). Triton X-114 extraction and partitioning experiments demonstrated that most Bdr paralogs are associated with the inner membrane-peptidoglycan complex. Analyses of cells treated with the highly chaotropic bile salt detergent deoxycholic acid demonstrated that some Bdr paralogs may also interact with the peptidoglycan, as evidenced by their tight association with the insoluble cellular matrix. In addition, immunoprecipitation (IP) experiments revealed an enhanced IP of all Bdr paralogs when the cell lysates were boiled prior to addition of the precipitating antibody. Furthermore, some Bdr paralogs were accessible to antibody in the IP experiments only in the boiled cell lysates. These observations suggest that different Bdr paralogs may carry out different structural-functional roles. Demonstration of the inner membrane localization of the Bdr proteins and of the differences in nature of the interaction of individual Bdr paralogs with the cell infrastructure is an important step toward defining the functional role of this unique protein family in the genus Borrelia.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Medical College of Virginia at Virginia Commonwealth University, School of Medicine, Richmond, VA 23298-0678. Phone: (804) 828-3779. Fax: (804) 828-9946. E-mail: rmarconi{at}hsc.vcu.edu.

Journal of Bacteriology, August 2000, p. 4222-4226, Vol. 182, No. 15
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Pinne, M., Denker, K., Nilsson, E., Benz, R., Bergstrom, S. (2006). The BBA01 Protein, a Member of Paralog Family 48 from Borrelia burgdorferi, Is Potentially Interchangeable with the Channel-Forming Protein P13.. J. Bacteriol. 188: 4207-4217 [Abstract] [Full Text]  
  • Zhang, H., Marconi, R. T. (2005). Demonstration of Cotranscription and 1-Methyl-3-Nitroso-Nitroguanidine Induction of a 30-Gene Operon of Borrelia burgdorferi: Evidence that the 32-Kilobase Circular Plasmids Are Prophages. J. Bacteriol. 187: 7985-7995 [Abstract] [Full Text]  
  • Zhang, H., Raji, A., Theisen, M., Hansen, P. R., Marconi, R. T. (2005). bdrF2 of Lyme Disease Spirochetes Is Coexpressed with a Series of Cytoplasmic Proteins and Is Produced Specifically during Early Infection. J. Bacteriol. 187: 175-184 [Abstract] [Full Text]  
  • Shin, J. J., Bryksin, A. V., Godfrey, H. P., Cabello, F. C. (2004). Localization of BmpA on the Exposed Outer Membrane of Borrelia burgdorferi by Monospecific Anti-Recombinant BmpA Rabbit Antibodies. Infect. Immun. 72: 2280-2287 [Abstract] [Full Text]  
  • Roberts, D. M., Caimano, M., McDowell, J., Theisen, M., Holm, A., Orff, E., Nelson, D., Wikel, S., Radolf, J., Marconi, R. T. (2002). Environmental Regulation and Differential Production of Members of the Bdr Protein Family of Borrelia burgdorferi. Infect. Immun. 70: 7033-7041 [Abstract] [Full Text]  
  • McDowell, J. V., Sung, S. Y., Labandeira-Rey, M., Skare, J. T., Marconi, R. T. (2001). Analysis of Mechanisms Associated with Loss of Infectivity of Clonal Populations of Borrelia burgdorferi B31MI. Infect. Immun. 69: 3670-3677 [Abstract] [Full Text]  
  • Labandeira-Rey, M., Skare, J. T. (2001). Decreased Infectivity in Borrelia burgdorferi Strain B31 Is Associated with Loss of Linear Plasmid 25 or 28-1. Infect. Immun. 69: 446-455 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»