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Infection and Immunity, December 1998, p. 6045-6048, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Structural Requirements for Glycosaminoglycan Recognition by the Lyme Disease Spirochete, Borrelia burgdorferidagger

John M. Leong,1,* Douglas Robbins,1 Louis Rosenfeld,2 Biswajit Lahiri,3,Dagger and Nikhat Parveen1

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655,1 and Neonatal Research Laboratory, Division of Neonatology, Department of Pediatrics,2 and Department of Biochemistry and Molecular Biology,3 New York Medical College, Valhalla, New York 10595

Received 4 August 1998/Returned for modification 10 September 1998/Accepted 29 September 1998

Borrelia burgdorferi, the Lyme disease agent, binds glycosaminoglycans (GAGs) such as heparin, heparan sulfate, and dermatan sulfate. Heparin or heparan sulfate fractions separated by size or charge were tested for their ability to inhibit attachment of B. burgdorferi to Vero cells. GAG chains of increasing length and/or charge showed increasing inhibitory potency, and detectable heparin inhibition of bacterial binding required a minimum of 16 residues. The ability of a given heparin fraction to inhibit binding to Vero cells was strongly predictive of its ability to inhibit hemagglutination, suggesting that hemagglutination reflects the capacity of B. burgdorferi to bind to GAGs.

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

dagger This paper is dedicated to the memory of Isidore Danishefsky.

Dagger Present address: Department of Medicine, New York Medical College, Valhalla, NY 10595.

Infection and Immunity, December 1998, p. 6045-6048, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • 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]  
  • 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]  
  • Parveen, N., Robbins, D., Leong, J. M. (1999). Strain Variation in Glycosaminoglycan Recognition Influences Cell-Type-Specific Binding by Lyme Disease Spirochetes. Infect. Immun. 67: 1743-1749 [Abstract] [Full Text]  


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