Chimeric papillomavirus-like particles expressing a foreign epitope on capsid surface loops

Neutralization capsid epitopes are important determinants for antibody-medi ated immune protection against papillomavirus (PV) infection and induced di sease. Chimeric L1 major capsid proteins of the human PV type 16 (HPV-16) a nd the bovine PV type 1 (BPV-1) with a foreign peptide incorporated into se veral capsid surface loops self-assembled into pentamers or virus-like part icles (VLP). Binding patterns of neutralizing monoclonal antibodies (MAb) a nd immunization of mice confirmed (i) that regions around aa 282-286 and 35 1-355 contribute to neutralization epitopes and identified the latter regio n as an immunodominant site and (ii) that placing a foreign peptide in the context of an assembled structure markedly enhanced its immunogenicity. Pen tamers 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.