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Peptide display on Potato virus X: Molecular features of the coat protein-fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles

TitlePeptide display on Potato virus X: Molecular features of the coat protein-fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2006
AuthorsLico, Chiara, Capuano F., Renzone G., Donini Marcello, Marusic Carla, Scaloni A., Benvenuto Eugenio, and Baschieri Selene
JournalJournal of General Virology
Volume87
Pagination3103 - 3112
Date Published2006
ISBN Number00221317 (ISSN)
KeywordsAmino Acid Sequence, amino terminal sequence, article, Capsid Proteins, coat protein, controlled study, DNA modification, drug formulation, expression vector, Genetic engineering, isoelectric point, Movement, mutation, nonhuman, peptide, phloem, Plant leaves, plant virus, Plasmids, Potato virus X, Potexvirus, priority journal, protein expression, protein subunit, Recombinant Fusion Proteins, Tobacco, tryptophan, virus gene, virus genome, virus infection, virus isolation, virus mutant, virus particle, virus vaccine
Abstract

The potexvirus Potato virus X(PVX) can be modified genetically to generate chimeric virus particles (CVPS) carrying heterologous peptides fused to coat protein (CP) subunits. A spontaneous PVX mutant expressing a truncated, but functional, form of the CP has been isolated. With the aim of exploiting this virus to display peptides useful for vaccine formulations, two novel viral expression vectors based on pPVX201 (bearing the wild-type PVX genome) were constructed encoding the truncated CP. Both vectors were able to produce infectious virus particles in planta and were used to insert a panel of sequences encoding pepticles of biopharmaceutical interest as N-terminal fusions to the truncated cp gene. The analysis of infection progression induced by the different constructs enabled identification of two important structural features of the fused peptide, namely tryptophan content and isoelectric point, critically affecting the formation of PVX CVPs and virus movement through the plant. These results are discussed in view of the rising interest in engineered plant viruses for development of peptide-based epitope vaccines. © 2006 SGM.

Notes

Cited By :35Export Date: 17 July 2015CODEN: JGVIACorrespondence Address: Baschieri, S.; Sezione di Genetica e Genomica Vegetale, ENEA CR Casaccia, Via Anguillarese 301, 00060 Rome, Italy; email: selene.baschieri@casaccia.enea.itChemicals/CAS: tryptophan, 6912-86-3, 73-22-3; Capsid Proteins; Recombinant Fusion ProteinsReferences: Atabekov, J.G., Rodionova, N.P., Karpova, O.V., Kozlovsky, S.V., Novikov, V.K., Arkhipenko, V., Translational activation of encapsidated potato virus X RNA by coat protein phosphorylation (2001) Virology, 286, pp. 466-474;Baratova, L.A., Grebenshchikov, N.I., Dobrov, E.N., The organization of potato virus X coat proteins in virus particles studied by tritium planigraphy and model building (1992) Virology, 188, pp. 175-180. , & 7 other authors; Baratova, L.A., Grebenshchikov, N.I., Shishkov, A.V., Kashirin, I.A., Radavsky, Y.L., Järvekülg, L., Saarma, M., The topography of the surface of potato virus X: Tritium planigraphy and immunological analysis (1992) J Gen Virol, 73, pp. 229-235; Baratova, L.A., Fedorova, N.V., Dobrov, E.N., N-terminal segment of potato virus X coat protein subunits is glycosylated and mediates formation of a bound water shell on the virion surface (2004) Eur J Biochem, 271, pp. 3136-3145. , & 7 other authors; Baulcombe, D.C., Chapman, S., Santa Cruz, S., Jellyfish green fluorescent protein as a reporter for virus infections (1995) Plant J, 7, pp. 1045-1053; Bendahmane, M., Koo, M., Karrer, E., Beachy, R.N., Display of epitopes on the surface of tobacco mosaic virus: Impact of charge and isoelectric point of the epitope on virus-host interactions (1999) J Mol Biol, 290, pp. 9-20; Borisova, G., Borschukova, O., Skrastina, D., Dislers, A., Ose, V., Pumpens, P., Grens, E., Behavior of a short preS1 epitope on the surface of hepatitis B core particles (1999) Biol Chem, 380, pp. 315-324; Brennan, F.R., Jones, T.D., Longstaff, M., Chapman, S., Bellaby, T., Smith, H., Xu, F., Flock, J.I., Immunogenicity of peptides derived from a fibronectin-binding protein of S. aureus expressed on two different plant viruses (1999) Vaccine, 17, pp. 1846-1857; Chapman, S., Kavanagh, T., Baulcombe, D., Potato virus X as a vector for gene expression in plants (1992) Plant J, 2, pp. 549-557; Chapman, S., Hills, G., Watts, J., Baulcombe, D., Mutational analysis of the coat protein gene of potato virus X: Effects on virion morphology and viral pathogenicity (1992) Virology, 191, pp. 223-230; Chen, Y.-T., Scanlan, M.J., Sahin, U., A testicular antigen aberrantly expressed in human cancers detected by autologous antibody screening (1997) Proc Natl Acad Sci U S A, 94, pp. 1914-1918. , & 7 other authors; Donini, M., Lico, C., Baschieri, S., Conti, S., Magliani, W., Polonelli, L., Benvenuto, E., Production of an engineered killer peptide in Nicotiana benthamiana by using a Potato virus X expression system (2005) Appl Environ Microbiol, 71, pp. 6360-6367; Fedorkin, O.N., Solovyev, A.G., Yelina, N.E., Zamyatnin Jr., A.A., Zinovkin, R.A., Mikinen, K., Schiemann, J., Morozov, S.Yu., Cell-to-cell movement of potato virus X involves distinct functions of the coat protein (2001) J Gen Virol, 82, pp. 449-458; Hurwitz, J.L., Slobod, K.S., Lockey, T.D., Wang, S., Chou, T.-H.W., Lu, S., Application of the polyvalent approach to HIV-1 vaccine development (2005) Curr Drug Targets Infect Disord, 5, pp. 143-156; Kimalov, B., Gal-On, A., Stav, R., Belausov, E., Arazi, T., Maintenance of coat protein N-terminal net charge and not primary sequence is essential for zucchini yellow mosaic virus systemic infectivity (2004) J Gen Virol, 85, pp. 3421-3430; Kirkin, A.L., Dzhandzhugazyan, K., Zeuthen, J., Melanoma-associated antigens recognized by cytotoxic T lymphocytes (1998) APMIS, 106, pp. 665-679; Koenig, R., Torrance, L., Antigenic analysis of potato virus X by means of monoclonal antibodies (1986) J Gen Virol, 67, pp. 2145-2151; Kozlovsky, S.V., Karpova, O.V., Arkhipenko, M.V., Zayakina, O.V., Rodionova, N.P., Atabekov, I.G., Effect of the N-terminal domain of the coat protein of Potato virus X on the structure of viral particles (2003) Dokl Biochem Biophys, 391, pp. 189-191; Lee, A.G., Lipid-protein interactions in biological membranes: A structural perspective (2003) Biochim Biophys Acta, 1612, pp. 1-40; Lesemann, D.E., Cytopathology (1988) The Plant Viruses: The Filamentous Plant Viruses, pp. 179-235. , Edited by R. 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