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Structure and assembly of the Ebola virus nucleocapsid
Ebola and Marburg viruses are filoviruses: filamentous, enveloped viruses that cause hemorrhagic fever1. Filoviruses are within the order Mononegavirales2 which also includes rabies virus, measles virus, and respiratory syncytial virus. Mononegaviruses have non-segmented, single-stranded negative-se...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5714281/ https://www.ncbi.nlm.nih.gov/pubmed/29144446 http://dx.doi.org/10.1038/nature24490 |
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author | Wan, William Kolesnikova, Larissa Clarke, Mairi Koehler, Alexander Noda, Takeshi Becker, Stephan Briggs, John A. G. |
author_facet | Wan, William Kolesnikova, Larissa Clarke, Mairi Koehler, Alexander Noda, Takeshi Becker, Stephan Briggs, John A. G. |
author_sort | Wan, William |
collection | PubMed |
description | Ebola and Marburg viruses are filoviruses: filamentous, enveloped viruses that cause hemorrhagic fever1. Filoviruses are within the order Mononegavirales2 which also includes rabies virus, measles virus, and respiratory syncytial virus. Mononegaviruses have non-segmented, single-stranded negative-sense RNA genomes that are encapsidated by nucleoprotein (NP) and other viral proteins to form a helical nucleocapsid (NC). NC acts as a scaffold for virus assembly and as a template for genome transcription and replication. Insights into NP-NP interactions have been derived from structural studies of oligomerized, RNA-encapsidating NP3–6 and cryo-electron microscopy (cryo-EM) of NC7–12 or NC-like structures11–13. There have been no high-resolution reconstructions of complete mononegavirus NCs. Here, we have applied cryo-electron tomography and subtomogram averaging to determine the structure of Ebola virus NC within intact viruses and recombinant NC-like assemblies. These structures reveal the identity and arrangement of the NC components, and suggest that the formation of an extended alpha-helix from the disordered C-terminal region of NP-core links NP oligomerization, NC condensation, RNA encapsidation, and accessory protein recruitment. |
format | Online Article Text |
id | pubmed-5714281 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
record_format | MEDLINE/PubMed |
spelling | pubmed-57142812018-05-08 Structure and assembly of the Ebola virus nucleocapsid Wan, William Kolesnikova, Larissa Clarke, Mairi Koehler, Alexander Noda, Takeshi Becker, Stephan Briggs, John A. G. Nature Article Ebola and Marburg viruses are filoviruses: filamentous, enveloped viruses that cause hemorrhagic fever1. Filoviruses are within the order Mononegavirales2 which also includes rabies virus, measles virus, and respiratory syncytial virus. Mononegaviruses have non-segmented, single-stranded negative-sense RNA genomes that are encapsidated by nucleoprotein (NP) and other viral proteins to form a helical nucleocapsid (NC). NC acts as a scaffold for virus assembly and as a template for genome transcription and replication. Insights into NP-NP interactions have been derived from structural studies of oligomerized, RNA-encapsidating NP3–6 and cryo-electron microscopy (cryo-EM) of NC7–12 or NC-like structures11–13. There have been no high-resolution reconstructions of complete mononegavirus NCs. Here, we have applied cryo-electron tomography and subtomogram averaging to determine the structure of Ebola virus NC within intact viruses and recombinant NC-like assemblies. These structures reveal the identity and arrangement of the NC components, and suggest that the formation of an extended alpha-helix from the disordered C-terminal region of NP-core links NP oligomerization, NC condensation, RNA encapsidation, and accessory protein recruitment. 2017-11-08 2017-11-16 /pmc/articles/PMC5714281/ /pubmed/29144446 http://dx.doi.org/10.1038/nature24490 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Wan, William Kolesnikova, Larissa Clarke, Mairi Koehler, Alexander Noda, Takeshi Becker, Stephan Briggs, John A. G. Structure and assembly of the Ebola virus nucleocapsid |
title | Structure and assembly of the Ebola virus nucleocapsid |
title_full | Structure and assembly of the Ebola virus nucleocapsid |
title_fullStr | Structure and assembly of the Ebola virus nucleocapsid |
title_full_unstemmed | Structure and assembly of the Ebola virus nucleocapsid |
title_short | Structure and assembly of the Ebola virus nucleocapsid |
title_sort | structure and assembly of the ebola virus nucleocapsid |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5714281/ https://www.ncbi.nlm.nih.gov/pubmed/29144446 http://dx.doi.org/10.1038/nature24490 |
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