Abstract
Turnip mosaic virus (TuMV), a potyvirus, is a flexible filamentous plant virus that displays a helical arrangement of coat protein copies (CPs) bound to the ssRNA genome. TuMV is a bona fide representative of the Potyvirus genus, one of most abundant groups of plant viruses, which displays a very wide host range. We have studied by cryoEM the structure of TuMV virions and its viral-like particles (VLPs) to explore the role of the interactions between proteins and RNA in the assembly of the virions. The results show that the CP-RNA interaction is needed for the correct orientation of the CP N-terminal arm, a region that plays as a molecular staple between CP subunits in the fully assembled virion.
Highlights
Turnip mosaic virus (TuMV), a potyvirus, is a flexible filamentous plant virus that displays a helical arrangement of coat protein copies (CPs) bound to the ssRNA genome
In this work we explore the structure of TuMV virions and viral-like particles (VLPs) to unveil the differences in their architecture and understand the contribution of protein-RNA interactions in the assembly of the virions
Using cryoEM and following single particle-based helical image processing, we have explored the structure of the potyvirus TuMV and its VLPs
Summary
Turnip mosaic virus (TuMV), a potyvirus, is a flexible filamentous plant virus that displays a helical arrangement of coat protein copies (CPs) bound to the ssRNA genome. We observe that TuMV VLPs produced in plants conserve the helical architecture of the virion and that the absence of the ssRNA precludes the interaction between CP subunits mediated by the N-terminal arm.
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