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Infection and Immunity, May 2001, p. 3455-3459, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3455-3459.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Delineation of Borrelia burgdorferi p66 Sequences Required for Integrin alpha IIbbeta 3 Recognition

Gillianne Defoe and Jenifer Coburn*

Division of Rheumatology and Immunology, Tufts-New England Medical Center, Boston, Massachusetts 02111

Received 18 December 2000/Returned for modification 2 February 2001/Accepted 7 February 2001

The outer membrane protein p66 of the Lyme disease agent, Borrelia burgdorferi, has been identified as a candidate ligand for beta 3-chain integrins. To identify portions of p66 required for integrin recognition, fusions of maltose-binding protein to fragments of p66 were tested for binding to integrin alpha IIbbeta 3, and synthetic peptides derived from the p66 amino acid sequence were tested for the ability to inhibit B. burgdorferi attachment to the same integrin. The data identify two noncontiguous segments of p66 that are important for alpha IIbbeta 3 recognition, suggesting that, as is true for other integrin ligands, the tertiary structure of p66 is important for receptor recognition.

* 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.

Infection and Immunity, May 2001, p. 3455-3459, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3455-3459.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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