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

 Previous Article  |  Next Article 

Infect. Immun., Mar 1995, 874-883, Vol 63, No. 3
Copyright © 1995, American Society for Microbiology

Hemagglutination and proteoglycan binding by the Lyme disease spirochete, Borrelia burgdorferi

JM Leong, PE Morrissey, E Ortega-Barria, ME Pereira and J Coburn
Division of Rheumatology and Immunology, Tufts-New England Medical Center Hospital, Boston, Massachusetts.

The ability of the Lyme disease spirochete to attach to host components may contribute to its ability to infect diverse tissues. We present evidence that the Lyme disease spirochete expresses a lectin activity that promotes agglutination of erythrocytes and bacterial attachment to glycosaminoglycans. Among a diverse collection of 21 strains of Lyme disease spirochete, hemagglutinating activity was easily detected in all but 3 strains, and these three strains were noninfectious. The ability to agglutinate erythrocytes was associated with the ability of the spirochete to bind to the sulfated polysaccharide dextran sulfate and to mammalian cells. Soluble dextran sulfate was a potent inhibitor of both hemagglutination and attachment to mammalian cells, while dextran had no effect on either activity, suggesting that dextran sulfate may inhibit attachment by mimicking host cell glycosaminoglycans. Consistent with this, the spirochete bound to immobilized heparin, and soluble heparin inhibited bacterial adhesion to mammalian cells. The bacterium did not bind efficiently to Vero cells treated with heparinase or heparitinase or to mutant CHO cell lines that are deficient in proteoglycan synthesis. Sulfation of glycosaminoglycans was critical for efficient bacterial recognition, as Vero cells treated with an inhibitor of sulfation, or a mutant CHO cell line that produces undersulfated heparan sulfate, did not mediate maximal spirochetal binding. Binding of the spirochete to extracellular matrix also appeared to be dependent upon this attachment pathway. These findings suggest that a glycosaminoglycan-binding activity which can be detected by hemagglutination contributes to the attachment of the Lyme disease spirochete to host cells and matrix.

This article has been cited by other articles:

• Sethi, N., Sondey, M., Bai, Y., Kim, K. S., Cadavid, D. (2006). Interaction of a Neurotropic Strain of Borrelia turicatae with the Cerebral Microcirculation System. Infect. Immun. 74: 6408-6418 [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]  
• Craig-Mylius, K., Weber, G. F., Coburn, J., Glickstein, L. (2005). Borrelia burgdorferi, an extracellular pathogen, circumvents osteopontin in inducing an inflammatory cytokine response. J. Leukoc. Biol. 77: 710-718 [Abstract] [Full Text]  
• Fadel, S., Eley, A. (2004). Chlorate: a reversible inhibitor of proteoglycan sulphation in Chlamydia trachomatis-infected cells. J Med Microbiol 53: 93-95 [Abstract] [Full Text]  
• Coburn, J., Cugini, C. (2003). Targeted mutation of the outer membrane protein P66 disrupts attachment of the Lyme disease agent, Borrelia burgdorferi, to integrin {alpha}v{beta}3. Proc. Natl. Acad. Sci. USA 100: 7301-7306 [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]  
• Cinco, M., Cini, B., Murgia, R., Presani, G., Prodan, M., Perticarari, S. (2001). Evidence of Involvement of the Mannose Receptor in Adhesion of Borrelia burgdorferi to Monocyte/Macrophages. Infect. Immun. 69: 2743-2747 [Abstract] [Full Text]  
• Ntchobo, H., Rothermel, H., Chege, W., Steere, A. C., Coburn, J. (2001). Recognition of Multiple Antibody Epitopes throughout Borrelia burgdorferi p66, a Candidate Adhesin, in Patients with Early or Late Manifestations of Lyme Disease. Infect. Immun. 69: 1953-1956 [Abstract] [Full Text]  
• Stephens, R. S., Fawaz, F. S., Kennedy, K. A., Koshiyama, K., Nichols, B., van Ooij, C., Engel, J. N. (2000). Eukaryotic Cell Uptake of Heparin-Coated Microspheres: a Model of Host Cell Invasion by Chlamydia trachomatis. Infect. Immun. 68: 1080-1085 [Abstract] [Full Text]  
• Coleman, J. L., Roemer, E. J., Benach, J. L. (1999). Plasmin-Coated Borrelia burgdorferi Degrades Soluble and Insoluble Components of the Mammalian Extracellular Matrix. Infect. Immun. 67: 3929-3936 [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]  
• Ortega-Barria, E., Boothroyd, J. C. (1999). A Toxoplasma Lectin-like Activity Specific for Sulfated Polysaccharides Is Involved in Host Cell Infection. J. Biol. Chem. 274: 1267-1276 [Abstract] [Full Text]  
• Leong, J. M., Robbins, D., Rosenfeld, L., Lahiri, B., Parveen, N. (1998). Structural Requirements for Glycosaminoglycan Recognition by the Lyme Disease Spirochete, Borrelia burgdorferi. Infect. Immun. 66: 6045-6048 [Abstract] [Full Text]  
• Coburn, J., Magoun, L., Bodary, S. C., Leong, J. M. (1998). Integrins alpha vbeta 3 and alpha 5beta 1 Mediate Attachment of Lyme Disease Spirochetes to Human Cells. Infect. Immun. 66: 1946-1952 [Abstract] [Full Text]  
• Leong, J. M., Wang, H., Magoun, L., Field, J. A., Morrissey, P. E., Robbins, D., Tatro, J. B., Coburn, J., Parveen, N. (1998). Different Classes of Proteoglycans Contribute to the Attachment of Borrelia burgdorferi to Cultured Endothelial and Brain Cells. Infect. Immun. 66: 994-999 [Abstract] [Full Text]