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Infect Immun, May 1998, p. 1946-1952, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Integrins alpha vbeta 3 and alpha 5beta 1 Mediate Attachment of Lyme Disease Spirochetes to Human Cells

Jenifer Coburn,1,* Loranne Magoun,2 Sarah C. Bodary,3 and John M. Leong2

Division of Rheumatology and Immunology, Tufts-New England Medical Center, Boston, Massachusetts 021111; Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, Worcester, Massachusetts 016552; and Department of Immunology, Genentech, Inc., South San Francisco, California 940803

Received 17 October 1997/Returned for modification 8 December 1997/Accepted 20 February 1998

Borrelia burgdorferi (sensu lato), the agent of Lyme disease, is able to cause chronic, multisystemic infections in human and animal hosts. Attachment of the spirochete to host cells is likely to be important for the colonization of diverse tissues. The platelet-specific integrin alpha IIbbeta 3 was previously identified as a receptor for all three species of Lyme disease spirochetes (B. burgdorferi sensu stricto, B. garinii, and B. afzelii). Here we show that B. burgdorferi also recognizes the widely expressed integrins alpha vbeta 3 and alpha 5beta 1, known as the vitronectin and fibronectin receptors, respectively. Three representatives of each species of Lyme disease spirochete were tested for the ability to bind to purified alpha vbeta 3 and alpha 5beta 1. All of the strains tested bound to at least one integrin. Binding to one integrin was not always predictive of binding to other integrins, and several different integrin preference profiles were identified. Attachment of the infectious B. burgdorferi strain N40 to purified alpha vbeta 3 and alpha 5beta 1 was inhibited by RGD peptides and the appropriate receptor-specific antibodies. Binding to alpha vbeta 3 was also shown by using a transfected cell line that expresses this receptor but not alpha IIbbeta 3. Attachment of B. burgdorferi N40 to human erythroleukemia cells and to human saphenous vein endothelial cells was mediated by both alpha 5beta 1 and alpha vbeta 3. Our results show that multiple integrins mediate attachment of Lyme disease spirochetes to host cells.

* Corresponding author. Mailing address: Division of Rheumatology and Immunology, Tufts-New England Medical Center, Box 406, 750 Washington St., Boston, MA 02111. Phone: (617) 636-5952. Fax: (617) 636-4252. E-mail: jcoburn_bor{at}opal.tufts.edu.

Infect Immun, May 1998, p. 1946-1952, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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