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Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement

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Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement

dc.contributor.author	Herranz, M. Carmen
dc.contributor.author	Sánchez Navarro, Jesús A.
dc.contributor.author	Saurí Peris, Ana
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Pallás Benet, Vicente
dc.date.accessioned	2018-04-13T13:49:12Z
dc.date.available	2018-04-13T13:49:12Z
dc.date.issued	2005
dc.identifier.citation	Herranz, M. Carmen Sánchez Navarro, Jesús A. Saurí Peris, Ana Mingarro Muñoz, Ismael Pallás Benet, Vicente 2005 Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement Virology 339 1 31 41
dc.identifier.uri	http://hdl.handle.net/10550/65661
dc.description.abstract	The movement protein (MP) of Prunus necrotic ringspot virus (PNRSV) is required for cell-to-cell movement. MP subcellular localization studies using a GFP fusion protein revealed highly punctate structures between neighboring cells, believed to represent plasmodesmata. Deletion of the RNA-binding domain (RBD) of PNRSV MP abolishes the cell-to-cell movement. A mutational analysis on this RBD was performed in order to identify in vivo the features that govern viral transport. Loss of positive charges prevented the cell-to-cell movement even though all mutants showed a similar accumulation level in protoplasts to those observed with the wild-type (wt) MP. Synthetic peptides representing the mutants and wild-type RBDs were used to study RNA-binding affinities by EMSA assays being approximately 20-fold lower in the mutants. Circular dichroism analyses revealed that the secondary structure of the peptides was not significantly affected by mutations. The involvement of the affinity changes between the viral RNA and the MP in the viral cell-to-cell movement is discussed.
dc.language.iso	eng
dc.relation.ispartof	Virology, 2005, vol. 339, num. 1, p. 31-41
dc.subject	Proteïnes
dc.subject	Virus
dc.title	Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement
dc.type	journal article	es_ES
dc.date.updated	2018-04-13T13:49:12Z
dc.identifier.doi	10.1016/j.virol.2005.05.020
dc.identifier.idgrec	020389
dc.rights.accessRights	open access	es_ES