Helical capsids of plant viruses: architecture with structural lability.
Capsids of numerous filamentous and rod-shaped plant viruses possess helical symmetry. In positive-stranded RNA viruses, helical capsids are typically composed of many identical subunits of the viral capsid protein (CP), encapsidating a molecule of viral genomic RNA. Current progress in structural studies of helical plant viruses has revealed differences between filamentous and rod-shaped viruses, both in structural folds of their CPs and in the interactions of CP molecules in their capsids. Many filamentous and rod-shaped viruses have functionally similar lateral inter-subunit contacts on the outer virion surface. Additionally, the extreme N-terminal CP region in filamentous viruses is intrinsically disordered. Taken together, the available data establish a link between the structural features of molecular interactions of CP molecules and the physical properties of helical virions ranging from rigidity to flexibility. Overall, the structure of helical plant viruses is significantly more labile than previously thought, often allowing structural transitions, remodelling and the existence of alternative structural forms of virions. These properties of virions are believed to be functionally significant at certain stages of the viral life cycle, such as during translational activation and cell-to-cell transport. In this review, we discuss structural and functional features of filamentous and rod-shaped virions, highlight their shared features and differences, and lay emphasis on the relationships between the molecular structure of viral capsids and their properties including virion shape, lability and capability of structural remodelling.
A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia.
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AG
Solovyev
A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia.
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Makarov
D002213:Capsid / Q000502:physiology* / Q000648:ultrastructure*; D036022:Capsid Proteins / Q000378:metabolism*; D010942:Plant Viruses / Q000502:physiology* / Q000648:ultrastructure*; D011485:Protein Binding; D019065:Virus Assembly
D036022:Capsid Proteins