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Cowpea mosaic virus is a plant-infecting member of the  Picornavirales  and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of  Picornavirales  capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 Å and 3.0 Å resolution, respectively, and built  de novo  atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which was missing from previously determined crystal structures, as well as residues that bind to the viral genome. These observations allow us to develop a new model for genome encapsidation and capsid assembly.

Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM