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

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 hel...

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Bibliographic Details
Published in:Science advances 2017-09, Vol.3 (9), p.eaao2182-eaao2182
Main Authors: Zamora, Miguel, Méndez-López, Eduardo, Agirrezabala, Xabier, Cuesta, Rebeca, Lavín, José L, Sánchez-Pina, M Amelia, Aranda, Miguel A, Valle, Mikel
Format: Article
Language:English
Subjects:
Binding Sites
Capsid Proteins - chemistry
Capsid Proteins - metabolism
Cryoelectron Microscopy
Models, Molecular
Nucleotide Motifs
Plant Viruses
Potyvirus - ultrastructure
Protein Binding
Protein Conformation
Protein Folding
RNA, Viral - chemistry
RNA, Viral - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
SciAdv r-articles
Viral Proteins - chemistry
Viral Proteins - metabolism
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Summary: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.
ISSN:2375-2548
2375-2548
DOI:10.1126/sciadv.aao2182