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

eLife

Mikel Valle¹  Gorka Lasso¹  Eduardo Méndez-López²  Miguel Aranda²  M Amelia Sánchez-Pina³  Xabier Agirrezabala⁴ 

[1] Consejo Superior de Investigaciones Científicas, Murcia, Spain;Centro de Edafología y Biología Aplicada del Segura, Murcia, Spain;Department of Biochemistry and Molecular Biophysics, Columbia University, New York, United States;Structural Biology Unit, Center for Cooperative Research in Biosciences, Derio, Spain;

关键词: flexible plant virus;    coat protein;    ssRNA viruses;    cryoEM;   

DOI  :  10.7554/eLife.11795

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown