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TitlePotyvirus virion structure shows conserved protein fold and RNA binding site in ssRNA viruses.
Journal, issue, pagesSci Adv, Vol. 3, Issue 9, Page eaao2182, Year 2017
Publish dateSep 20, 2017
AuthorsMiguel Zamora / Eduardo Méndez-López / Xabier Agirrezabala / Rebeca Cuesta / José L Lavín / M Amelia Sánchez-Pina / Miguel A Aranda / Mikel Valle /
PubMed AbstractPotyviruses 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. ...Potyviruses 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.
External linksSci Adv / PubMed:28948231 / PubMed Central
MethodsEM (helical sym.)
Resolution4.0 Å
Structure data

3785

5odv

EMDB-3785, PDB-5odv:
Structure of Watermelon mosaic virus potyvirus.
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • watermelon mosaic virus
KeywordsVIRUS / filamentous virus / potyvirus / plant pathogen

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