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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, C., Lico Chiara, Maffi D., D'Angeli S., Altamura M.M., Benvenuto Eugenio, Faoro F., and Baschieri Selene
JournalMolecular Plant Pathology
Volume13
Pagination198-203
ISSN14646722
KeywordsAmino Acid Sequence, article, capsid protein, Capsid Proteins, chemistry, coat protein, cytology, Evans blue, metabolism, molecular genetics, Molecular Sequence Data, Movement, movement (physiology), mutant protein, Mutant Proteins, Nicotiana benthamiana, physiology, plant leaf, Plant leaves, Potato virus X, Potexvirus, recombinant protein, Recombinant Proteins, Tobacco, Ultrastructure, Virology
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. © 2011.

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URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84855756173&doi=10.1111%2fj.1364-3703.2011.00739.x&partnerID=40&md5=81cfd2e71cc42b816cdb143d6cce612e
DOI10.1111/j.1364-3703.2011.00739.x
Citation KeyBetti2012198