Transient expression of foreign
genes based on
plant viral vectors is a suitable system for the
production of relevant immunogens that can be used for the development of a new generation of
vaccines against a variety of
infectious diseases. In the present study the
epitope derived from HPV-16 L2
minor capsid protein (
amino acids 108–120) was expressed from
Potato virus X (PVX)-based vector pGR106 as N- or C-terminal fusion with the PVX coat
protein (PVX CP) in transgenic
Nicotiana benthamiana
plants. The fusion
protein L2108-120-PVX CP was successfully expressed in
plants at a level of 170 mg/kg of fresh leaf
tissue. The C-terminal fusion
protein PVX CP- L2108-120 was expressed using mutated vector sequence to avoid
homologous recombination at a level of 8 mg/kg of fresh leaf
tissue. Immunogenicity of L2108-120-PVX CP
virus-like particles was tested after
immunization of
mice by
subcutaneous injection or
tattoo administration. In
animal sera the
antibodies against the PVX CP and the L2108-120
epitope were found after both
methods of
vaccine delivery.