Immunogenicity of a Multiepitope Plasmid DNA Encoding T and B Lymphocyte Epitopes from Latent Membrane Protein 2 (LMP2) of Epstein-Barr Virus as a Vaccine in Mice
Epstein-Barr virus (EBV) is a human oncogenic herpesvirus associating with several malignant diseases. Latent membrane protein 2 (LMP2) of EBV is considered to be an ideal candidate for immunotherapy or prophylactic EBV vaccine. We designed a LMP2 multiepitope containing T and B-cell
epitope-rich peptides and constructed a recombinant plasmid containing mammalian codonoptimization EBV LMP2 multiepitope (pcDNA3.1(+)/EBV-LMP2 multiepitope). After pcDNA3.1(+)/EBV-LMP2 multiepitope was transfected into COS-7 cells, significant expression of the multiepitope in COS-7 cells
was confirmed by RT-PCR and immunofluorescence assay. Western blot analysis indicated that serum from immunized mice could be discerned by the EBV-LMP2 protein and the EBV-LMP2 multiepitope specifically. The plasmid DNA of EBV-LMP2 multiepitope induced high levels anti-EBV membrane protein
and anti-EBV LMP2 multiepitope IgG in mice. T lymphocytes from spleen of immunized mice showed a strong CTL activity. The present study suggested that plasmid DNA encoding EBV LMP2 multiepitope capable of stimulating enough cellular and humoral immunity could have potential for preventing
or controlling EBV infection and EBV associated disease in mice.
Keywords: DNA vaccine; EBV; LMP2; multiepitope
Document Type: Research Article
Publication date: 01 October 2013
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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