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Potyvirus virion structure shows conserved protein fold and RNA binding site in ssRNA viruses

AutorZamora, Miguel; Méndez-López, Eduardo; Agirrezabala, Xabier; Cuesta, Rebeca; Lavín, José L.; Sánchez-Pina, M. Amelia ; Aranda, Miguel A. ; Valle, Mikel
Fecha de publicación1-sep-2017
EditorAmerican Association for the Advancement of Science
CitaciónScience Advances 3(9): eaao2182 (2017)
ResumenPotyviruses constitute the second largest genus of plant viruses and cause important economic losses in a large variety of crops; however, the atomic structure of their particles remains unknown. Infective potyvirus virions are long flexuous filaments where coat protein (CP) subunits assemble in helical mode bound to a monopartite positive-sense single-stranded RNA [(+)ssRNA] genome. We present the cryo-electron microscopy (cryoEM) structure of the potyvirus watermelon mosaic virus at a resolution of 4.0 Å. The atomic model shows a conserved fold for the CPs of flexible filamentous plant viruses, including a universally conserved RNA binding pocket, which is a potential target for antiviral compounds. This conserved fold of the CP is widely distributed in eukaryotic viruses and is also shared by nucleoproteins of enveloped viruses with segmented (−)ssRNA (negative-sense ssRNA) genomes, including influenza viruses.
Versión del editorhttp://dx.doi.org/10.1126/sciadv.aao2182
URIhttp://hdl.handle.net/10261/163537
DOI10.1126/sciadv.aao2182
E-ISSN2375-2548
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