Program Schedule

1352
Progression of Lyme Disease to Later Stages is Associated with Antibody Response Towards the Membrane-Proximal Domain of the VlsE Protein of Borrelia burgdorferi

Session: Poster Abstract Session: Biomarkers of Immune Responses
Saturday, October 11, 2014
Room: The Pennsylvania Convention Center: IDExpo Hall BC
Posters
  • IID poster 2014_Ela-2final copy.pdf (1.1 MB)
  • Background: Lyme disease is associated with a robust B cell response to the VlsE lipoprotein of Borrelia burgdorferi.  Epitope mapping analyses have shown the IR6 region within the variable domain and specific sequences in the N- and C-terminal invariable domains of VlsE to contain the major immunogenic regions.  However, antibody reactivity against immunodominant epitopes of VlsE has not been systematically analyzed during the various stages of infection. 

    Methods: Here, we examined serum samples from 90 patients with a range of early to late manifestations of Lyme borreliosis for antibody reactivity to the three major epitope sequences of VlsE.  These included amino acid sequences 274-298 (IR6 epitope), 21-44 (N-terminal epitope), and 336-349 (C-terminal epitope) of the VlsE protein from B. burgdorferi B31. In addition, antibody response to a recombinantly generated protein containing the entire membrane-proximal domain of VlsE and its associated epitopes as a contiguous sequence was examined. 

    Results: Antibody reactivity to the IR6 region of VlsE was found to vary little between cohorts of patients representing early disseminated to late manifestations of Lyme disease.  In contrast, antibody responses towards the specific N- and C-terminal epitopes of VlsE, as well as the recombinant sequence representing the entire membrane-proximal region, were predominantly absent during early Lyme disease and became highly elevated in late manifestations. 

    Conclusion: The data help to elucidate the evolution of humoral immune reactivity to VlsE during the course of B. burgdorferi infection, demonstrating the development of a divergent antibody response towards distinct epitopes of a single protein.  The results may be consequential to gaining an understanding of the epitopes’ potential involvement in a mechanism of immune evasion by the spirochetes.

    Elzbieta Jacek1, Lars Komorowsky2, Mary Ajamian1, Brad Kim1, Gary P. Wormser, MD3, Adriana Marques, MD4 and Armin Alaedini1, (1)Columbia University, New York, NY, (2)Institute for Experimental Immunology, Lubeck, Germany, (3)New York Medical College, Valhalla, NY, (4)NIH, Bethesda, MD

    Disclosures:

    E. Jacek, None

    L. Komorowsky, None

    M. Ajamian, None

    B. Kim, None

    G. P. Wormser, None

    A. Marques, None

    A. Alaedini, None

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