Acta NaturaeActa NaturaeActa Naturae2075-8251Acta Naturae Ltd1065810.32607/20758251-2011-3-4-73-82ArticlesСтатьиResearch ArticleNew Viral Vector for Superproduction of Epitopes of Vaccine Proteins in PlantsNew Viral Vector for Superproduction of Epitopes of Vaccine Proteins in PlantsTyulkinaL G

Faculty of Biology

SkuratE V

Faculty of Biology

FrolovaO YuKomarovaT VKargerE MAtabekovI G

Faculty of Biology

atabekov@genebee.msu.suLomonosov Moscow State UniversityBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University1512201134VOL 3, NO4 (2011)ТОМ 3, №4 (2011)738217012020Copyright ©; 2011, Tyulkina L.G., Skurat E.V., Frolova O.Y., Komarova T.V., Karger E.M., Atabekov I.G.Copyright ©; 2011, Tyulkina L.G., Skurat E.V., Frolova O.Y., Komarova T.V., Karger E.M., Atabekov I.G.2011Tyulkina L.G., Skurat E.V., Frolova O.Y., Komarova T.V., Karger E.M., Atabekov I.G.Tyulkina L.G., Skurat E.V., Frolova O.Y., Komarova T.V., Karger E.M., Atabekov I.G.https://creativecommons.org/licenses/by/4.0https://actanaturae.ru/2075-8251/article/view/10658

The novel viral vectors PVX-CP AltMV and PVXdt-CP AltMV are superexpressors of the capsid protein (CP). These viral vectors were constructed on the basis of the potato virus X (PVX) genome and Alternanthera mosaic virus (AltMV) CP gene. The expression, based on the hybrid viral vectors, is genetically safe, since the systemic transport and formation of infective viral particles are blocked. CP AltMV can self-assemble into virus-like particles (VLPs) in the absence of genomic RNA. The vectors can be used for the presentation of foreign peptides (including epitopes of human pathogens) on the surface of the VLP. The N-terminal extracellular domain (M2e) of the influenza virus A M2 protein and its truncated variant (ΔM2e) were used as model heterologous peptides for the construction of the chimeric CP AltMV. Chimeric CP AltMV retains its ability to self-assemble into VLP. The epitopes of the M2 influenza virus protein were not eliminated during the process of accumulation, polymerization and purification of chimeric VLP AltMV, providing evidence of the stability of chimeric VLP with C-terminal heterologous epitopes. It appears that VLP produced by the vectors PVX-CP AltMV and PVXdt-CP AltMV can be used in the field of biotechnology for the presentation of the epitopes of vaccine proteins on their surfaces. The chimeric VLP AltMV with the presented foreign epitopes can be used as candidate vaccines.

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