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Infect Immun, March 1998, p. 994-999, Vol. 66, No. 3
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Different Classes of Proteoglycans Contribute to the Attachment of Borrelia burgdorferi to Cultured Endothelial and Brain Cells

John M. Leong,1,* Hong Wang,1 Loranne Magoun,1 Jodie A. Field,2 Pamela E. Morrissey,2 Douglas Robbins,1 Jeffrey B. Tatro,3 Jenifer Coburn,2 and Nikhat Parveen1

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655,1 and Division of Rheumatology and Immunology2 and Division of Endocrinology, Metabolism, Diabetes and Molecular Medicine,3 Department of Medicine and the Tupper Research Institute, Tufts- New England Medical Center, Boston, Massachusetts 02111

Received 27 October 1997/Returned for modification 19 November 1997/Accepted 10 December 1997

The Lyme disease spirochete, Borrelia burgdorferi, infects multiple tissues, such as the heart, joint, skin, and nervous system and has been shown to recognize heparan sulfate and dermatan sulfate proteoglycans. In this study, we examined the contribution of different classes of proteoglycans to the attachment of the infectious B. burgdorferi strain N40 to several immortalized cell lines and primary cultured cells, including endothelial cells and brain cells. Bacterial attachment was inhibited by exogenous proteoglycans or by treatment of host cells with inhibitors of proteoglycan synthesis or sulfation, indicating that proteoglycans play a critical role in bacterial binding to diverse cell types. Binding to primary bovine capillary endothelial cells or a human endothelial cell line was also inhibited by digestion with heparinase or heparitinase but not with chondroitinase ABC. In contrast, binding to glial cell-enriched brain cell cultures or to a neuronal cell line was inhibited by all three lyases. Binding of strain N40 to immobilized heparin could be completely inhibited by dermatan sulfate, and conversely, binding to dermatan sulfate could be completely blocked by heparin. As measured by 50% inhibitory dose, heparin was a better inhibitor of binding than dermatan sulfate, regardless of whether the substrate was heparin or dermatan sulfate. These results are consistent with the hypotheses that the species of proteoglycans recognized by B. burgdorferi vary with cell type and that bacterial recognition of different proteoglycans is mediated by the same bacterial molecule(s).

* 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.




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