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Journal of Clinical Microbiology, April 2000, p. 1569-1574, Vol. 38, No. 4
0095-1137/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Borrelia burgdorferi B31 Erp Proteins
That Are Dominant Immunoblot Antigens of Animals Infected with
Isolate B31 Are Recognized by Only a Subset of Human Lyme
Disease Patient Sera
Jennifer C.
Miller,
Nazira
El-Hage,
Kelly
Babb, and
Brian
Stevenson*
Department of Microbiology and Immunology,
University of Kentucky College of Medicine, Lexington, Kentucky
40536-0084
Received 20 October 1999/Returned for modification 24 December
1999/Accepted 20 January 2000
Sera from animals infected with Borrelia burgdorferi
isolates yield intense immunoblot signals from the B31 ErpA/I/N and
ErpB/J/O proteins, which have apparent molecular masses of 19 and 60 kDa, respectively. Since B. burgdorferi proteins with those
molecular masses are of immunodiagnostic importance, Lyme disease
patient sera were used in studies of B31 lysates and recombinant B31
ErpA/I/N and ErpB/J/O proteins. Immunoblot analyses indicated that only a minority of the patients produced antibodies that recognized the
tested B31 Erp proteins. Southern blot analyses of Lyme disease spirochetes cultured from 16 of the patients indicated that all these
bacteria contain genes related to the B31 erpA/I/N and
erpB/J/O genes, although signal strengths indicated only
weak similarities in many cases, suggestive of genetic variability of
erp genes among these bacteria. These data indicate that
Erp proteins are generally not the 19- and 60-kDa antigens observed on
serodiagnostic immunoblots.
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, MS 415 Chandler Medical Center, University of Kentucky College of Medicine, Lexington, KY 40536-0084. Phone: (606)
257-9358. Fax: (606) 257-8994. E-mail:
bstev0{at}pop.uky.edu.
Journal of Clinical Microbiology, April 2000, p. 1569-1574, Vol. 38, No. 4
0095-1137/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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