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Journal of Clinical Microbiology, December 1999, p. 3997-4004, Vol. 37, No. 12
0095-1137/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Human Antibody Responses to VlsE Antigenic Variation Protein of Borrelia burgdorferi

M. B. Lawrenz,1 J. M. Hardham,1,dagger R. T. Owens,2 J. Nowakowski,3 A. C. Steere,4 G. P. Wormser,3 and S. J. Norris1,*

Departments of Pathology and Laboratory Medicine and Microbiology and Molecular Genetics, University of Texas Medical School at Houston,1 and Institute of Biosciences and Technology, Texas A & M University,2 Houston, Texas; Department of Medicine, Division of Infectious Disease, New York Medical College, Valhalla, New York3; and Division of Rheumatology/Immunology, Tufts University School of Medicine, New England Medical Center, Tupper Research Institute, Boston, Massachusetts4

Received 22 March 1999/Returned for modification 29 April 1999/Accepted 13 September 1999

VlsE is a 35-kDa surface-exposed lipoprotein of Borrelia burgdorferi that was shown previously to undergo antigenic variation through segmental recombination of silent vls cassettes with vlsE during experimental mouse infections. Previous data had indicated that sera from North American Lyme disease patients and experimentally infected animals contained antibodies reactive with VlsE. In this study, sera from patients with Lyme disease, syphilis, and autoimmune conditions as well as from healthy controls were examined for reactivity with VlsE by Western blotting and enzyme-linked immunosorbent assay (ELISA). Strong Western blot reactivity to a recombinant VlsE cassette region protein was obtained consistently with Lyme disease sera. Although sera from Lyme disease patients also reacted with a band corresponding to VlsE in B. burgdorferi B31-5A3, interpretation was complicated by low levels of VlsE expression in in vitro-cultured B. burgdorferi and by the presence of comigrating bands. An ELISA using recombinant VlsE was compared with an ELISA using sonically disrupted B. burgdorferi as the antigen. For a total of 93 Lyme disease patient sera examined, the VlsE ELISA yielded sensitivities of 63% for culture-confirmed erythema migrans cases and 92% for later stages, as compared to 61 and 98%, respectively, for the "whole-cell" ELISA. The specificities of the two assays with healthy blood donor sera were comparable, but the VlsE ELISA was 90% specific with sera from syphilis patients, compared to 20% specificity for the whole-cell ELISA with this group. Neither assay showed reactivity with a panel of sera from 20 non-Lyme disease arthritis patients or 20 systemic lupus erythematosus patients. Our results indicate that VlsE may be useful in the immunodiagnosis of Lyme disease and may offer greater specificity than ELISAs using whole B. burgdorferi as the antigen.

* Corresponding author. Mailing address: Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin, Houston, TX 77030. Phone: (713) 500-5338. Fax: (713) 500-0730. E-mail: norr{at}casper.med.uth.tmc.edu.

dagger Present address: Animal Health Biological Discovery, Pfizer, Inc., Groton, Conn.

Journal of Clinical Microbiology, December 1999, p. 3997-4004, Vol. 37, No. 12
0095-1137/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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