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Chimeric papillomavirus-like particles expressing a foreign epitope on capsid surface loops
Katharina Slupetzky1, Saeed Shafti-Keramat1, Petra Lenz1
1Laboratory of Viral Oncology, Division of Immunology, Allergy and Infectious Diseases (DIAID)1, and Division of General Dermatology, Department of Dermatology2, University of Vienna Medical School, Währinger Gürtel 18-20, A-1090 Vienna, Austria.
Abstract:
Neutralization capsid epitopes are important determinants for antibody-mediated immune protection against papillomavirus (PV) infection and induced disease. Chimeric L1 major capsid proteins of the human PV type 16 (HPV-16) and the bovine PV type 1 (BPV-1) with a foreign peptide incorporated into several capsid surface loops self-assembled into pentamers or virus-like particles (VLP). Binding patterns of neutralizing monoclonal antibodies (MAb) and immunization of mice confirmed (i) that regions around aa 282-286 and 351-355 contribute to neutralization epitopes and identified the latter region as an immunodominant site and (ii) that placing a foreign peptide in the context of an assembled structure markedly enhanced its immunogenicity. Pentamers disassembled from wild-type HPV-16 and BPV-1 VLPs displayed some of the neutralization epitopes that were detected on fully assembled VLPs, but were deficient for binding a subset of neutralizing MAb that inhibit cell attachment.