Recognition of multiple antibody epitopes throughout Borrelia burgdorferi p66, a candidate adhesin, in patients with early or late manifestations of Lyme disease. Infect Immun 2001 Mar;69(3):1953-6
Date
02/17/2001Pubmed ID
11179382Pubmed Central ID
PMC98111DOI
10.1128/IAI.69.3.1953-1956.2001Scopus ID
2-s2.0-0035112447 (requires institutional sign-in at Scopus site) 21 CitationsAbstract
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 beta3-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.
Author List
Ntchobo H, Rothermel H, Chege W, Steere AC, Coburn JAuthor
Jenifer Coburn PhD, MA Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Antibodies, BacterialBacterial Proteins
Borrelia burgdorferi Group
Epitopes
Humans
Immunoglobulin G
Immunoglobulin M
Lyme Disease
Porins
Time Factors
