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 Parveen, N.
Right arrow Articles by Leong, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Parveen, N.
Right arrow Articles by Leong, J. M.

 Previous Article  |  Next Article 

Infection and Immunity, April 1999, p. 1743-1749, Vol. 67, No. 4
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Strain Variation in Glycosaminoglycan Recognition Influences Cell-Type-Specific Binding by Lyme Disease Spirochetes

Nikhat Parveen, Douglas Robbins, and John M. Leong*

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655

Received 17 September 1998/Returned for modification 25 November 1998/Accepted 1 January 1999

Lyme disease, a chronic multisystemic disorder that can affect the skin, heart, joints, and nervous system is caused by Borrelia burgdorferi sensu lato. Lyme disease spirochetes were previously shown to bind glycosaminoglycans (GAGs). In the current study, the GAG-binding properties of eight Lyme disease strains were determined. Binding by two high-passage HB19 derivatives to Vero cells could not be inhibited by enzymatic removal of GAGs or by the addition of exogenous GAG. The other six strains, which included a different high-passage HB19 derivative (HB19 clone 1), were shown to recognize both heparan sulfate and dermatan sulfate in cell-binding assays, but the relative efficiency of binding to these two GAGs varied among the strains. Strains N40, CA20-2A, and PBi bound predominantly to heparan sulfate, PBo bound both heparan sulfate and dermatan sulfate roughly equally, and VS461 and HB19 clone 1 recognized primarily dermatan sulfate. Cell binding by strain HB19 clone 1 was inhibited better by exogenous dermatan sulfate than by heparin, whereas heparin was the better inhibitor of binding by strain N40. The GAG-binding preference of a Lyme disease strain was reflected in its cell-type-specific binding. Strains that recognized predominantly heparan sulfate bound efficiently to both C6 glioma cells and EA-Hy926 cells, whereas strains that recognized predominantly dermatan sulfate bound well only to the glial cells. The effect of lyase treatment of these cells on bacterial binding was consistent with the model that cell-type-specific binding was a reflection of the GAG-binding preference. We conclude that the GAG-binding preference varies with the strain of Lyme disease spirochete and that this variation influences cell-type-specific binding in vitro.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, 55 Lake Avenue North, Worcester, MA 01655. Phone: (508) 856-4059. Fax: (508) 856-5920. E-mail: john.leong{at}banyan.ummed.edu.

Infection and Immunity, April 1999, p. 1743-1749, Vol. 67, No. 4
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Shi, Y., Xu, Q., McShan, K., Liang, F. T. (2008). Both Decorin-Binding Proteins A and B Are Critical for the Overall Virulence of Borrelia burgdorferi. Infect. Immun. 76: 1239-1246 [Abstract] [Full Text]  
  • Xu, Q., Seemanaplli, S. V., McShan, K., Liang, F. T. (2007). Increasing the Interaction of Borrelia burgdorferi with Decorin Significantly Reduces the 50 Percent Infectious Dose and Severely Impairs Dissemination. Infect. Immun. 75: 4272-4281 [Abstract] [Full Text]  
  • Shi, Y., Xu, Q., Seemanapalli, S. V., McShan, K., Liang, F. T. (2006). The dbpBA Locus of Borrelia burgdorferi Is Not Essential for Infection of Mice. Infect. Immun. 74: 6509-6512 [Abstract] [Full Text]  
  • Fischer, J. R., LeBlanc, K. T., Leong, J. M. (2006). Fibronectin Binding Protein BBK32 of the Lyme Disease Spirochete Promotes Bacterial Attachment to Glycosaminoglycans. Infect. Immun. 74: 435-441 [Abstract] [Full Text]  
  • Liang, F. T., Brown, E. L., Wang, T., Iozzo, R. V., Fikrig, E. (2004). Protective Niche for Borrelia burgdorferi to Evade Humoral Immunity. Am. J. Pathol. 165: 977-985 [Abstract] [Full Text]  
  • Zambrano, M. C., Beklemisheva, A. A., Bryksin, A. V., Newman, S. A., Cabello, F. C. (2004). Borrelia burgdorferi Binds to, Invades, and Colonizes Native Type I Collagen Lattices. Infect. Immun. 72: 3138-3146 [Abstract] [Full Text]  
  • Fischer, J. R., Parveen, N., Magoun, L., Leong, J. M. (2003). Decorin-binding proteins A and B confer distinct mammalian cell type-specific attachment by Borrelia burgdorferi, the Lyme disease spirochete. Proc. Natl. Acad. Sci. USA 100: 7307-7312 [Abstract] [Full Text]  
  • Bretz, A. G., Ryffel, K., Hutter, P., Dayer, E., Peter, O. (2001). Specificities and Sensitivities of Four Monoclonal Antibodies for Typing of Borrelia burgdorferi Sensu Lato Isolates. CVI 8: 376-384 [Abstract] [Full Text]  
  • Wang, G., van Dam, A. P., Schwartz, I., Dankert, J. (1999). Molecular Typing of Borrelia burgdorferi Sensu Lato: Taxonomic, Epidemiological, and Clinical Implications. Clin. Microbiol. Rev. 12: 633-653 [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»