http://www.cnr.it/ontology/cnr/individuo/prodotto/ID200227

Potato virus X movement in Nicotiana benthamiana: new details revealed by chimeric coat protein variants (Articolo in rivista)

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Potato virus X movement in Nicotiana benthamiana: new details revealed by chimeric coat protein variants (Articolo in rivista) (literal)

Anno

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Alternative label

Betti C., Lico C., Maffi D., D'Angeli S., Altamura M.M., Benvenuto E., Faoro F., Baschieri S. (2012)
Potato virus X movement in Nicotiana benthamiana: new details revealed by chimeric coat protein variants
in MPPOL. Molecular plant pathology on-line; BSPP, British society for plant pathology, Reading (Regno Unito)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Betti C., Lico C., Maffi D., D'Angeli S., Altamura M.M., Benvenuto E., Faoro F., Baschieri S. (literal)

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Note

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BC, LC, BE, BS: Unità Tecnica Biologia delle Radiazioni e Salute dell'Uomo, Laboratorio di Biotecnologie, ENEA C.R. Casaccia, Roma, Italia DS, AMM : Dipartimento di Biologia Vegetale, Università 'Sapienza' di Roma, Roma Italia MD, FF: Dipartimento di Produzione Vegetale, Università degli Studi di Milano, Milan0, Italia FF: CNR, IVV, Torino, Italia (literal)

Titolo

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

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 (literal)

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