NATURE COMMUNICATIONS | ARTICLE OPEN
Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM
Emma L. Hesketh, Yulia Meshcheriakova, Kyle C. Dent, Pooja Saxena, Rebecca F. Thompson, Joseph J. Cockburn, George P. Lomonossoff & Neil A. Ranson
Affiliations Contributions Corresponding author
Nature Communications 6, Article number: 10113 doi:10.1038/ncomms10113
Received 06 August 2015 Accepted 03 November 2015 Published 10 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.
Subject terms: Biological sciences Virology Biotechnology
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