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Infection and Immunity, March 2001, p. 1953-1956, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1953-1956.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Recognition of Multiple Antibody Epitopes throughout Borrelia burgdorferi p66, a Candidate Adhesin, in Patients with Early or Late Manifestations of Lyme Disease

Hyacinthe Ntchobo, Holly Rothermel, Wambui Chege, Allen C. Steere, and Jenifer Coburn*

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

Received 10 October 2000/Returned for modification 10 November 2000/Accepted 28 November 2000

Antibody responses to p66, a candidate integrin ligand of Borrelia burgdorferi, were studied in 79 patients with early or late manifestations of Lyme disease. The central portion of p66 was previously shown to contain all of the information required for specific recognition of beta 3-chain integrins, but work by others had suggested that the C-terminal portion of the protein contains a single surface-exposed, immunodominant loop. In examining antibody responses to full-length p66 and to three overlapping fragments of the protein, we found that the majority of Lyme disease patients had immunoglobulin M (IgM) and/or IgG responses to p66 and that, particularly early in the disease, epitopes throughout p66 were recognized. Among patients with later manifestations of the illness, antibody responses to the C-terminal portion of the protein were more prominent. These results demonstrate that Lyme disease patient sera recognize epitopes throughout p66.

* 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, March 2001, p. 1953-1956, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1953-1956.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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