Obtaining and characterization of spherical particles—new biogenic platforms
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Lico, C., Mancini, C., Italiani, P., Betti, C., Boraschi, D., Benvenuto, E., and Bashieri, S., Plantproduced potato virus X chimeric particles displaying an influenza virus-derived peptide activate specific CD8+ T cells in mice, Vaccine, 2009, vol. 27, no. 37, pp. 5069–5076.
Karpova, O., Nikitin, N., Chirkov, S., Trifonova, E., Sheveleva, A., Lazareva, E., and Atabekov, J., Immunogenic compositions assembled from tobacco mosaic virus-generated spherical particle platform and foreign antigens, J. Gen. Virol., 2012, vol. 93, no. 2, pp. 400–407.
Nikitin, N., Trifonova, E., Karpova, O., and Atabekov, J., Examination of biologically active nanocomplexes by nanoparticle tracking analysis, Microsc. Microanal., 2013, vol. 19, no. 4, pp. 808–813.
Trifonova, E., Nikitin, N., Gmyl, A., Lazareva, E., Karpova, O., and Atabekov, J., Complexes assembled from TMV-derived spherical particles and entire virions of heterogeneous nature, J. Biomol. Struct. Dyn., 2014, vol. 32, no. 8, pp. 1193–1201.
Nikitin, N.A., Malinin, A.S., Trifonova, E.A., Rakhnyanskaya, A.A., Yaroslavov, A.A., Karpova, O.V., and Atabekov, J.G., Proteins immobilization on the surface of modified plant viral particles coated with hydrophobic polycations, J. Biomat. Sci. Polym. Ed., 2014, vol. 25, no. 16, pp. 1743–1754.
Soto, C.M. and Ratna, B.R., Virus hybrids as nanomaterials for biotechnology, Curr. Opin. Biotechnol., 2010, vol. 21, no. 4, pp. 426–438.
Leong, H.S., Steinmetz, N.F., Ablack, A., Destito, G., Zijlstra, A., Stuhlmann, H., Manchester, M., and Lewis, J.D., Intravital imaging of embryonic and tumor neovasculature using viral nanoparticles, Nat. Protoc., 2010, vol. 5, no. 8, pp. 1406–1417.
Bruckman, M.A., Hern, S., Jiang, K., Flask, C.A., Yu, X., and Steinmetz, N.F., Tobacco mosaic virus rods and spheres as supramolecular high-relaxivity MRI contrast agents, J. Mater. Chem. B. Mater. Biol. Med., 2013 vol. 1, no. 10, pp. 1482–1490.
Aljabali, A.A., Shukla, S., Lomonossoff, G.P., Steinmetz, N.F., and Evans, D.J., CPMV-DOX delivers, Mol. Pharm., 2013, vol. 10, no. 1, pp. 3–10.
Lebel, M.E., Daudelin, J.F., Chartrand, K., Tarrab, E., Kalinke, U., Savard, P., Labrecque, N., Leclerc, D., and Lamarre, A., Nanoparticle adjuvant sensing by TLR7 enhances CD8+ T cell-mediated protection from Listeria monocytogenes infection, J. Immunol., 2014, vol. 192, no. 3, pp. 1071–1078.
Atabekov, J., Nikitin, N., Arkhipenko, M., Chirkov, S., and Karpova, O., Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles, J. Gen. Virol., 2011, vol. 92, no. 2, pp. 453–456.
Nikitin, N.A., Malinin, A.S., Rakhnyanskaya, A.A., Trifonova, E.A., Karpova, O.V., Yaroslavov, A.A., and Atabekov, J.G., Use of a polycation spacer for noncovalent immobilization of albumin on thermally modified virus particles, Polym. Sci. Ser. A, 2011, vol. 53, no. 11, pp. 1026–1031.
Bruckman, M.A., VanMeter, A., and Steinmetz N.F., Nanomanufacturing of tobacco mosaic virus-based spherical biomaterials using a continuous flow method, ACS Biomater. Sci. Eng., 2015, vol. 1, no. 1, pp. 13–18.
Volkova, E.G., Kurchashova, S.Y., Polyakov, V.Y., and Sheval, E.V., Self-organization of cellular structures induced by the overexpression of nuclear envelope proteins: a correlative light and electron microscopy study, J. Electron Microsc., 2011, vol. 60, no. 1, pp. 57–71.
ASTM Standard E2834, 2012. ASTM International. West Conshohocken. PA, 2012.
Loh, E., Ralston, E., and Schumaker, V.N., Quasielastic light scattering from solutions of filamentous viruses. I. Experimental, Biopolymers, 1979, vol. 18, no. 10, pp. 2549–2567.
Sano, Y., Translational diffusion coefficient of tobacco mosaic virus particles, J. Gen. Virol., 1987, vol. 68, no. 9, pp. 2439–2442.
Dobrov, E.N., Nikitin, N.A., Trifonova, E.A., Parshina, E.Y., Makarov, V.V., Maksimov, G.V., Karpova, O.V., and Atabekov, J.G., β-Structure of the coat protein subunits in spherical particles generated by tobacco mosaic virus thermal denaturation, J. Biomol. Struct. Dyn., 2014, vol. 32, no. 5, pp. 701–708.