Transient expression of Human papillomavirus type 16 L2 epitope fused to N- and C-terminus of coat protein of Potato virus X in plants
Language English Country India Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Epitopes genetics metabolism MeSH
- Genetic Vectors genetics MeSH
- Plants, Genetically Modified MeSH
- Immunization MeSH
- Cloning, Molecular MeSH
- Humans MeSH
- Plant Leaves metabolism MeSH
- Mice, Inbred C57BL MeSH
- Mice MeSH
- Oligonucleotides genetics MeSH
- Oncogene Proteins, Viral metabolism MeSH
- Antibodies, Viral blood MeSH
- Recombinant Fusion Proteins immunology metabolism MeSH
- Nicotiana metabolism MeSH
- Microscopy, Electron, Transmission MeSH
- Virion immunology MeSH
- Capsid Proteins metabolism MeSH
- Blotting, Western MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- coat protein, Potato virus X MeSH Browser
- Epitopes MeSH
- L2 protein, Human papillomavirus type 16 MeSH Browser
- Oligonucleotides MeSH
- Oncogene Proteins, Viral MeSH
- Antibodies, Viral MeSH
- Recombinant Fusion Proteins MeSH
- Capsid Proteins MeSH
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 L2 108-120-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- L2 108-120 was expressed using mutated vector sequence to avoid homologous recombination at a level of 8 mg/kg of fresh leaf tissue. Immunogenicity of L2 108-120-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 L2 108-120 epitope were found after both methods of vaccine delivery.
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