Structure and Engineering of papaya mosaic virus nanoparticles

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Papaya mosaic virus (PapMV) is a flexuous rod shape plant virus that is the member of the potexvirus family. We are interested in the assembly process and the structure of this virus because it is a reference for all the other flexuous rod shape plant viruses. Recently, we have resolved the 3D structure of 80 per cent of the PapMV coat protein (CP) and identified important residues involved in the interaction between the protein subunits and the RNA backbone. In addition, we have developed an in vitro assembly assay based on the use of recombinant CP produced in E. coli allowing testing several mutants. Based on this unique expertise, we propose to further improve our understanding of the structure of the PapMV CP through directed mutations in the CP and test their ability to self-assemble into nanoparticles. This study will permit to confirm our model and further improve our understanding of the structure of this virus. We will give a special attention to the C-terminus of the PapMV CP and attempt to elucidate the structure of this 'missing part' of the PapMV CP 3D structure. We will attempt to confirm the parallel coiled-coil predicted by Bio-Informatic at the C terminus of the CP of this virus. Finally, our expertise on the structure of the PapMV CP will allow us developing a novel platform that will become the basement for the design of a new class of bactericide. It is anticipated that the fusion of antibacterial peptides (magainin) at the surface of PapMV nanoparticles will lead to engineered nanoparticles with improved anti-bacterial lytic activities. We will use mutated form of the CP that harbour improved stability to further increase the bactericide activity and the length of the period of storage of the nanoparticles. This research program is exciting because it combines fundamental aspects of the structure of the PapMV CP and the development and design of an innovative tool in nanotechnology.