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 and Neil A. Ranson ()
Additional contact information
Emma L. Hesketh: Astbury Centre for Structural Molecular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK
Yulia Meshcheriakova: John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK
Kyle C. Dent: Astbury Centre for Structural Molecular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK
Pooja Saxena: John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK
Rebecca F. Thompson: Astbury Centre for Structural Molecular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK
Joseph J. Cockburn: Astbury Centre for Structural Molecular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK
George P. Lomonossoff: John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK
Neil A. Ranson: Astbury Centre for Structural Molecular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: 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.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms10113 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10113

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms10113

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().