The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses

Flexible filamentous viruses include economically important plant pathogens. Their viral particles contain several hundred copies of a helically arrayed coat protein (CP) protecting a (+)ssRNA. We describe here a structure at 3.9 Å resolution, from electron cryomicroscopy, of Pepino mosaic virus (Pe...

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Bibliographic Details
Published in:eLife 2015-12, Vol.4, p.e11795-e11795
Main Authors: Agirrezabala, Xabier, Méndez-López, Eduardo, Lasso, Gorka, Sánchez-Pina, M Amelia, Aranda, Miguel, Valle, Mikel
Format: Article
Language:English
Subjects:
Biophysics and Structural Biology
Capsid Proteins - metabolism
Capsid Proteins - ultrastructure
coat protein
Cryoelectron Microscopy
cryoEM
flexible plant virus
Health aspects
Homology (Biology)
Host-virus relationships
Models, Molecular
Observations
Potexvirus - ultrastructure
Protein Binding
Protein Folding
RNA, Viral - metabolism
ssRNA viruses
Viral proteins
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Summary:Flexible filamentous viruses include economically important plant pathogens. Their viral particles contain several hundred copies of a helically arrayed coat protein (CP) protecting a (+)ssRNA. We describe here a structure at 3.9 Å resolution, from electron cryomicroscopy, of Pepino mosaic virus (PepMV), a representative of the genus Potexvirus (family Alphaflexiviridae). Our results allow modeling of the CP and its interactions with viral RNA. The overall fold of PepMV CP resembles that of nucleoproteins (NPs) from the genus Phlebovirus (family Bunyaviridae), a group of enveloped (-)ssRNA viruses. The main difference between potexvirus CP and phlebovirus NP is in their C-terminal extensions, which appear to determine the characteristics of the distinct multimeric assemblies - a flexuous, helical rod or a loose ribonucleoprotein. The homology suggests gene transfer between eukaryotic (+) and (-)ssRNA viruses.
ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.11795