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The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy
BACKGROUND: Filoviruses, including Ebola virus, are unusual in being filamentous animal viruses. Structural data on the arrangement, stoichiometry and organisation of the component molecules of filoviruses has until now been lacking, partially due to the need to work under level 4 biological contain...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256159/ https://www.ncbi.nlm.nih.gov/pubmed/22247782 http://dx.doi.org/10.1371/journal.pone.0029608 |
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author | Beniac, Daniel R. Melito, Pasquale L. deVarennes, Shauna L. Hiebert, Shannon L. Rabb, Melissa J. Lamboo, Lindsey L. Jones, Steven M. Booth, Timothy F. |
author_facet | Beniac, Daniel R. Melito, Pasquale L. deVarennes, Shauna L. Hiebert, Shannon L. Rabb, Melissa J. Lamboo, Lindsey L. Jones, Steven M. Booth, Timothy F. |
author_sort | Beniac, Daniel R. |
collection | PubMed |
description | BACKGROUND: Filoviruses, including Ebola virus, are unusual in being filamentous animal viruses. Structural data on the arrangement, stoichiometry and organisation of the component molecules of filoviruses has until now been lacking, partially due to the need to work under level 4 biological containment. The present study provides unique insights into the structure of this deadly pathogen. METHODOLOGY AND PRINCIPAL FINDINGS: We have investigated the structure of Ebola virus using a combination of cryo-electron microscopy, cryo-electron tomography, sub-tomogram averaging, and single particle image processing. Here we report the three-dimensional structure and architecture of Ebola virus and establish that multiple copies of the RNA genome can be packaged to produce polyploid virus particles, through an extreme degree of length polymorphism. We show that the helical Ebola virus inner nucleocapsid containing RNA and nucleoprotein is stabilized by an outer layer of VP24-VP35 bridges. Elucidation of the structure of the membrane-associated glycoprotein in its native state indicates that the putative receptor-binding site is occluded within the molecule, while a major neutralizing epitope is exposed on its surface proximal to the viral envelope. The matrix protein VP40 forms a regular lattice within the envelope, although its contacts with the nucleocapsid are irregular. CONCLUSIONS: The results of this study demonstrate a modular organization in Ebola virus that accommodates a well-ordered, symmetrical nucleocapsid within a flexible, tubular membrane envelope. |
format | Online Article Text |
id | pubmed-3256159 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-32561592012-01-13 The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy Beniac, Daniel R. Melito, Pasquale L. deVarennes, Shauna L. Hiebert, Shannon L. Rabb, Melissa J. Lamboo, Lindsey L. Jones, Steven M. Booth, Timothy F. PLoS One Research Article BACKGROUND: Filoviruses, including Ebola virus, are unusual in being filamentous animal viruses. Structural data on the arrangement, stoichiometry and organisation of the component molecules of filoviruses has until now been lacking, partially due to the need to work under level 4 biological containment. The present study provides unique insights into the structure of this deadly pathogen. METHODOLOGY AND PRINCIPAL FINDINGS: We have investigated the structure of Ebola virus using a combination of cryo-electron microscopy, cryo-electron tomography, sub-tomogram averaging, and single particle image processing. Here we report the three-dimensional structure and architecture of Ebola virus and establish that multiple copies of the RNA genome can be packaged to produce polyploid virus particles, through an extreme degree of length polymorphism. We show that the helical Ebola virus inner nucleocapsid containing RNA and nucleoprotein is stabilized by an outer layer of VP24-VP35 bridges. Elucidation of the structure of the membrane-associated glycoprotein in its native state indicates that the putative receptor-binding site is occluded within the molecule, while a major neutralizing epitope is exposed on its surface proximal to the viral envelope. The matrix protein VP40 forms a regular lattice within the envelope, although its contacts with the nucleocapsid are irregular. CONCLUSIONS: The results of this study demonstrate a modular organization in Ebola virus that accommodates a well-ordered, symmetrical nucleocapsid within a flexible, tubular membrane envelope. Public Library of Science 2012-01-11 /pmc/articles/PMC3256159/ /pubmed/22247782 http://dx.doi.org/10.1371/journal.pone.0029608 Text en Beniac et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Beniac, Daniel R. Melito, Pasquale L. deVarennes, Shauna L. Hiebert, Shannon L. Rabb, Melissa J. Lamboo, Lindsey L. Jones, Steven M. Booth, Timothy F. The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy |
title | The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy |
title_full | The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy |
title_fullStr | The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy |
title_full_unstemmed | The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy |
title_short | The Organisation of Ebola Virus Reveals a Capacity for Extensive, Modular Polyploidy |
title_sort | organisation of ebola virus reveals a capacity for extensive, modular polyploidy |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256159/ https://www.ncbi.nlm.nih.gov/pubmed/22247782 http://dx.doi.org/10.1371/journal.pone.0029608 |
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