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Potato virus X movement in Nicotiana benthamiana: new details revealed by chimeric coat protein variants.

TitlePotato virus X movement in Nicotiana benthamiana: new details revealed by chimeric coat protein variants.
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2012
AuthorsBetti, Camilla, Lico Chiara, Maffi Dario, D'Angeli Simone, Altamura Maria Maddalena, Benvenuto Eugenio, Faoro Franco, and Baschieri Selene
JournalMol Plant Pathol
Volume13
Issue2
Pagination198-203
Date Published2012 Feb
ISSN13643703
KeywordsAmino Acid Sequence, Capsid Proteins, Evans blue, Molecular Sequence Data, Movement, Mutant Proteins, Plant leaves, Potexvirus, Recombinant Proteins, Tobacco
Abstract

Potato virus X coat protein is necessary for both cell-to-cell and phloem transfer, but it has not been clarified definitively whether it is needed in both movement phases solely as a component of the assembled particles or also of differently structured ribonucleoprotein complexes. To clarify this issue, we studied the infection progression of a mutant carrying an N-terminal deletion of the coat protein, which was used to construct chimeric virus particles displaying peptides selectively affecting phloem transfer or cell-to-cell movement. Nicotiana benthamiana plants inoculated with expression vectors encoding the wild-type, mutant and chimeric viral genomes were examined by microscopy techniques. These experiments showed that coat protein-peptide fusions promoting cell-to-cell transfer only were not competent for virion assembly, whereas long-distance movement was possible only for coat proteins compatible with virus particle formation. Moreover, the ability of the assembled PVX to enter and persist into developing xylem elements was revealed here for the first time.

DOI10.1111/j.1364-3703.2011.00739.x
Alternate JournalMol. Plant Pathol.
Citation Key6043
PubMed ID21851552