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Diagnostic Laboratory Immunology

Outer Surface Protein C Peptide Derived from Borrelia burgdorferi Sensu Stricto as a Target for Serodiagnosis of Early Lyme Disease

Paul M. Arnaboldi, Rudra Seedarnee, Mariya Sambir, Steven M. Callister, Josephine A. Imparato, Raymond J. Dattwyler
Paul M. Arnaboldi
aBiopeptides Corp., East Setauket, New York, USA
bDepartment of Microbiology, New York Medical College, Valhalla, New York, USA
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Rudra Seedarnee
bDepartment of Microbiology, New York Medical College, Valhalla, New York, USA
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Mariya Sambir
aBiopeptides Corp., East Setauket, New York, USA
bDepartment of Microbiology, New York Medical College, Valhalla, New York, USA
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Steven M. Callister
cGundersen Lutheran Medical Center, La Crosse, Wisconsin, USA
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Josephine A. Imparato
aBiopeptides Corp., East Setauket, New York, USA
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Raymond J. Dattwyler
aBiopeptides Corp., East Setauket, New York, USA
bDepartment of Microbiology, New York Medical College, Valhalla, New York, USA
dDepartment of Medicine, New York Medical College, Valhalla, New York, USA
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DOI: 10.1128/CVI.00608-12
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ABSTRACT

Current serodiagnostic assays for Lyme disease are inadequate at detecting early infection due to poor sensitivity and nonspecificity that arise from the use of whole bacteria or bacterial proteins as assay targets; both targets contain epitopes that are cross-reactive with epitopes found in antigens of other bacterial species. Tests utilizing peptides that contain individual epitopes highly specific for Borrelia burgdorferi as diagnostic targets are an attractive alternative to current assays. Using an overlapping peptide library, we mapped linear epitopes in OspC, a critical virulence factor of B. burgdorferi required for mammalian infection, and confirmed the results by enzyme-linked immunosorbent assay (ELISA). We identified a highly conserved 20-amino-acid peptide epitope, OspC1. Via ELISA, OspC1 detected specific IgM and/or IgG in 60 of 98 serum samples (62.1%) obtained from patients with erythema migrans (early Lyme disease) at the time of their initial presentation. By comparison, the commercially available OspC peptide PepC10 detected antibody in only 48 of 98 serum samples (49.0%). In addition, OspC1 generated fewer false-positive results among negative healthy and diseased (rheumatoid arthritis and positive Rapid Plasma Reagin [RPR+] test result) control populations than did PepC10. Both highly specific and more sensitive than currently available OspC peptides, OspC1 could have value as a component of a multipeptide Lyme disease serological assay with significantly improved capabilities for the diagnosis of early infection.

FOOTNOTES

    • Received 18 October 2012.
    • Returned for modification 27 November 2012.
    • Accepted 2 January 2013.
    • Accepted manuscript posted online 30 January 2013.
  • Supplemental material for this article may be found at http://dx.doi.org/10.1128/CVI.00608-12.

  • Copyright © 2013, American Society for Microbiology. All Rights Reserved.
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Outer Surface Protein C Peptide Derived from Borrelia burgdorferi Sensu Stricto as a Target for Serodiagnosis of Early Lyme Disease
Paul M. Arnaboldi, Rudra Seedarnee, Mariya Sambir, Steven M. Callister, Josephine A. Imparato, Raymond J. Dattwyler
Clinical and Vaccine Immunology Mar 2013, 20 (4) 474-481; DOI: 10.1128/CVI.00608-12

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Outer Surface Protein C Peptide Derived from Borrelia burgdorferi Sensu Stricto as a Target for Serodiagnosis of Early Lyme Disease
Paul M. Arnaboldi, Rudra Seedarnee, Mariya Sambir, Steven M. Callister, Josephine A. Imparato, Raymond J. Dattwyler
Clinical and Vaccine Immunology Mar 2013, 20 (4) 474-481; DOI: 10.1128/CVI.00608-12
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