Potyviral coat protein polymorphism
The coat protein (CP) has many different roles in the life cycle of potyviruses, but the structural background of its multitasking remains unclear. We have performed a comprehensive high-resolution structural analysis of recombinant CP that has revealed a fascinatingly broad structural landscape of its self-assemblies. These can range from polymorphic flexuous filaments that can be redirected by simple modifications of CP to form filamentous particles with desired morphologies and molecular properties, to novel assemblies such as orthogonal cubic or spherical particles. We show that such structural transformations are enabled by the high frequency of structural disorder and the chaotic nature of CP. This intriguing structural susceptibility of CP appears to be the driving force for its multifunctionality, making CP an attractive molecular platform for bionanotechnology.