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Title: Further improvement of PVX/CMV CP expression tool for presentation of short foreign epitopes

Author
item NATILLA, ANGELA - UNIV OF BASILICATA ITALY
item Nemchinov, Lev

Submitted to: Protein Expression and Purification
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/14/2008
Publication Date: 5/1/2008
Citation: Natilla, A., Nemchinov, L.G. 2008. Further improvement of PVX/CMV CP expression tool for presentation of short foreign epitopes. Protein Expression and Purification. 59(1):117-121.

Interpretive Summary: Newcastle disease virus (NDV) is an economically important pathogen of poultry causing a fatal and highly contagious virus disease affecting most species of birds. Currently, vaccines against NDV are live viruses that can themselves cause mild disease, depending on co-infections with other diseases and environmental conditions. This study is a continuation of our previous research in developing an alternative anti-NDV vaccine that is safe and cost-effective. To achieve this, we chose a technology where high-level production of desired foreign proteins in the host plant results from a rapidly multiplying plant virus carrying a self-assembling plant virus shell which contains the foreign protective vaccine. This plant-produced protein has the potential for development into a candidate vaccine for vaccination of chicks against NDV. These results will be of interest to plant and animal researchers, and representatives of industry, academia, and government organizations with an interest in plant-based systems for production of vaccine, immunology, and veterinary health.

Technical Abstract: We have previously reported that Potato Virus X-expressed coat protein of Cucumber mosaic virus (CMV) formed virus-like particles (VLPs), which served as carriers for display of different neutralizing epitopes of Newcastle disease virus (NDV). In this work, we further modified the purification protocol of recombinant VLPs carrying short neutralizing epitope of NDV's hemagglutinin-neuraminidase protein and confirmed that transiently expressed from heterologous virus, self-contained capsid protein subunits of CMV package into individual virions morphologically resembling and/or indistinguishable from wild type CMV particles. Immunoblot analysis revealed that CMV VLPs efficiently presented imported epitope of animal virus.