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dc.contributor.author
Sánchez Eugenia, Rubén
dc.contributor.author
Durana, Aritz
dc.contributor.author
López Marijuan, Ibai
dc.contributor.author
Marti, Gerardo Anibal
dc.contributor.author
Guérin, Diego Marcelo Alejandro
dc.date.available
2018-06-18T16:11:57Z
dc.date.issued
2016-10
dc.identifier.citation
Sánchez Eugenia, Rubén; Durana, Aritz; López Marijuan, Ibai; Marti, Gerardo Anibal; Guérin, Diego Marcelo Alejandro; X-ray structure of Triatoma virus empty capsid: Insights into the mechanism of uncoating and RNA release in dicistroviruses; Society for General Microbiology; Journal of General Virology; 97; 10; 10-2016; 2769-2779
dc.identifier.issn
0022-1317
dc.identifier.uri
http://hdl.handle.net/11336/48999
dc.description.abstract
In viruses, uncoating and RNA release are two key steps of successfully infecting a target cell. During these steps, the capsid must undergo the necessary conformational changes to allow RNA egress. Despite their importance, these processes are poorly understood in the family Dicistroviridae. Here, we used X-ray crystallography to solve the atomic structure of a Triatoma virus(TrV) empty particle (Protein Data Bank ID 5L7O), which is the resulting capsid after RNA release. It is observed that the overall shape of the capsid and of the three individual proteins is maintained in comparison with the mature virion. Furthermore, no channels indicative of RNA release are formed in the TrV empty particle. However, the most prominent change in the empty particle when compared with the mature virion is the loss of order in the N-terminal domain of the VP2 protein. In mature virions, the VP2 N-terminal domain of one pentamer is swapped with its twofold related copy in an adjacent pentamer, thereby stabilizing the binding between the pentamers. The loss of these interactions allows us to propose that RNA release may take place through transient flipping-out of pentameric subunits. The lower number of stabilizing interactions between the pentamers and the lack of formation of new holes support this model. This model differs from the currently accepted model for rhinoviruses and enteroviruses, in which genome externalization occurs by extrusion of the RNA through capsid channels.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Society for General Microbiology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Capsid Disassembly
dc.subject
Dicistroviridae
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Rna Release
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Triatoma Virus
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Uncoating
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Otras Ciencias Biológicas
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
X-ray structure of Triatoma virus empty capsid: Insights into the mechanism of uncoating and RNA release in dicistroviruses
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-18T13:31:49Z
dc.journal.volume
97
dc.journal.number
10
dc.journal.pagination
2769-2779
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Sánchez Eugenia, Rubén. Instituto Biofisika; España
dc.description.fil
Fil: Durana, Aritz. Instituto Biofisika; España. Fundación Biofísica Bizkaia; España
dc.description.fil
Fil: López Marijuan, Ibai. Instituto Biofisika; España. Fundación Biofísica Bizkaia; España
dc.description.fil
Fil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina
dc.description.fil
Fil: Guérin, Diego Marcelo Alejandro. Instituto Biofisika; España. Universidad del País Vasco; España. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Journal of General Virology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1099/jgv.0.000580
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000580
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