TY - JOUR
T1 - The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses
AU - Agirrezabala, Xabier
AU - Méndez-López, Eduardo
AU - Lasso, Gorka
AU - Sánchez-Pina, M. Amelia
AU - Aranda, Miguel
AU - Valle, Mikel
N1 - Funding Information:
This work was supported by grants from the Spanish Ministry of Economy and Competitiveness (BFU2012-34873 and AGL2012-37390). FEM was the recipient of a FPI predoctoral fellowship from the Spanish Ministry of Economy and Competitiveness. We thank the Electron Microscopy Facility from the Laboratory of Molecular Biology (LMB-MRC, Cambridge) for the access to the electron microscope, Shaoxia Chen, Christos Savva, and Luis Rodríguez-Moreno for technical assistance.
Funding Information:
Ministry of Economy and Competitiveness BFU2012-34873 Mikel Valle, Ministry of Economy and Competitiveness AGL2012-37390 Miguel Aranda.
Publisher Copyright:
© Agirrezabala et al.
PY - 2015/12/16
Y1 - 2015/12/16
N2 - 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.
AB - 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.
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U2 - 10.7554/eLife.11795
DO - 10.7554/eLife.11795
M3 - Article
C2 - 26673077
AN - SCOPUS:84986002755
SN - 2050-084X
VL - 4
JO - eLife
JF - eLife
IS - DECEMBER2015
M1 - e11795
ER -