The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy

Abstract Cowpea mosaic virus (CPMV) is a picorna-like plant virus. As well as an intrinsic interest in CPMV as a plant pathogen, CPMV is of major interest in biotechnology applications such as nanotechnology. Here, we report high resolution cryo electron microscopy (cryo-EM) maps of wild type CPMV c...

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Autores principales: Emma L. Hesketh, Yulia Meshcheriakova, Rebecca F. Thompson, George P. Lomonossoff, Neil A. Ranson
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/5a08a9447f2247ffa6187b87a1890e27
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spelling oai:doaj.org-article:5a08a9447f2247ffa6187b87a1890e272021-12-02T11:52:27ZThe structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy10.1038/s41598-017-00533-w2045-2322https://doaj.org/article/5a08a9447f2247ffa6187b87a1890e272017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00533-whttps://doaj.org/toc/2045-2322Abstract Cowpea mosaic virus (CPMV) is a picorna-like plant virus. As well as an intrinsic interest in CPMV as a plant pathogen, CPMV is of major interest in biotechnology applications such as nanotechnology. Here, we report high resolution cryo electron microscopy (cryo-EM) maps of wild type CPMV containing RNA-2, and of naturally-formed empty CPMV capsids. The resolution of these structures is sufficient to visualise large amino acids. We have refined an atomic model for each map and identified an essential amino acid involved in genome encapsidation. This work has furthered our knowledge of Picornavirales genome encapsidation and will assist further work in the development of CPMV as a biotechnological tool.Emma L. HeskethYulia MeshcheriakovaRebecca F. ThompsonGeorge P. LomonossoffNeil A. RansonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Emma L. Hesketh
Yulia Meshcheriakova
Rebecca F. Thompson
George P. Lomonossoff
Neil A. Ranson
The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
description Abstract Cowpea mosaic virus (CPMV) is a picorna-like plant virus. As well as an intrinsic interest in CPMV as a plant pathogen, CPMV is of major interest in biotechnology applications such as nanotechnology. Here, we report high resolution cryo electron microscopy (cryo-EM) maps of wild type CPMV containing RNA-2, and of naturally-formed empty CPMV capsids. The resolution of these structures is sufficient to visualise large amino acids. We have refined an atomic model for each map and identified an essential amino acid involved in genome encapsidation. This work has furthered our knowledge of Picornavirales genome encapsidation and will assist further work in the development of CPMV as a biotechnological tool.
format article
author Emma L. Hesketh
Yulia Meshcheriakova
Rebecca F. Thompson
George P. Lomonossoff
Neil A. Ranson
author_facet Emma L. Hesketh
Yulia Meshcheriakova
Rebecca F. Thompson
George P. Lomonossoff
Neil A. Ranson
author_sort Emma L. Hesketh
title The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
title_short The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
title_full The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
title_fullStr The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
title_full_unstemmed The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
title_sort structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/5a08a9447f2247ffa6187b87a1890e27
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