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

DOI: 10.1038/ncomms10113 DOI Help

Authors: Emma L. Hesketh (University of Leeds) , Yulia Meshcheriakova (John Innes Centre) , Kyle C. Dent (Diamond Light Source) , Pooja Saxena (Indiana University) , Rebecca F. Thompson (University of Leeds) , Joseph J. Cockburn (University of Leeds) , George P. Lomonossoff (John Innes Centre) , Neil A. Ranson (University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 6

State: Published (Approved)
Published: December 2015

Abstract: 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.

Journal Keywords: Biological Sciences; Virology; Biotechnology

Subject Areas: Biology and Bio-materials


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