Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.

Several major human pathogens, including the filoviruses, paramyxoviruses, and rhabdoviruses, package their single-stranded RNA genomes within helical nucleocapsids, which bud through the plasma membrane of the infected cell to release enveloped virions. The virions are often heterogeneous in shape,...

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Autores principales:	Tanmay A M Bharat, James D Riches, Larissa Kolesnikova, Sonja Welsch, Verena Krähling, Norman Davey, Marie-Laure Parsy, Stephan Becker, John A G Briggs
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/add284b5168b49b7a8f0d8b2547f688e
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spelling	oai:doaj.org-article:add284b5168b49b7a8f0d8b2547f688e2021-11-18T05:36:54ZCryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.1544-91731545-788510.1371/journal.pbio.1001196https://doaj.org/article/add284b5168b49b7a8f0d8b2547f688e2011-11-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22110401/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Several major human pathogens, including the filoviruses, paramyxoviruses, and rhabdoviruses, package their single-stranded RNA genomes within helical nucleocapsids, which bud through the plasma membrane of the infected cell to release enveloped virions. The virions are often heterogeneous in shape, which makes it difficult to study their structure and assembly mechanisms. We have applied cryo-electron tomography and sub-tomogram averaging methods to derive structures of Marburg virus, a highly pathogenic filovirus, both after release and during assembly within infected cells. The data demonstrate the potential of cryo-electron tomography methods to derive detailed structural information for intermediate steps in biological pathways within intact cells. We describe the location and arrangement of the viral proteins within the virion. We show that the N-terminal domain of the nucleoprotein contains the minimal assembly determinants for a helical nucleocapsid with variable number of proteins per turn. Lobes protruding from alternate interfaces between each nucleoprotein are formed by the C-terminal domain of the nucleoprotein, together with viral proteins VP24 and VP35. Each nucleoprotein packages six RNA bases. The nucleocapsid interacts in an unusual, flexible "Velcro-like" manner with the viral matrix protein VP40. Determination of the structures of assembly intermediates showed that the nucleocapsid has a defined orientation during transport and budding. Together the data show striking architectural homology between the nucleocapsid helix of rhabdoviruses and filoviruses, but unexpected, fundamental differences in the mechanisms by which the nucleocapsids are then assembled together with matrix proteins and initiate membrane envelopment to release infectious virions, suggesting that the viruses have evolved different solutions to these conserved assembly steps.Tanmay A M BharatJames D RichesLarissa KolesnikovaSonja WelschVerena KrählingNorman DaveyMarie-Laure ParsyStephan BeckerJohn A G BriggsPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 9, Iss 11, p e1001196 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Tanmay A M Bharat James D Riches Larissa Kolesnikova Sonja Welsch Verena Krähling Norman Davey Marie-Laure Parsy Stephan Becker John A G Briggs Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.
description	Several major human pathogens, including the filoviruses, paramyxoviruses, and rhabdoviruses, package their single-stranded RNA genomes within helical nucleocapsids, which bud through the plasma membrane of the infected cell to release enveloped virions. The virions are often heterogeneous in shape, which makes it difficult to study their structure and assembly mechanisms. We have applied cryo-electron tomography and sub-tomogram averaging methods to derive structures of Marburg virus, a highly pathogenic filovirus, both after release and during assembly within infected cells. The data demonstrate the potential of cryo-electron tomography methods to derive detailed structural information for intermediate steps in biological pathways within intact cells. We describe the location and arrangement of the viral proteins within the virion. We show that the N-terminal domain of the nucleoprotein contains the minimal assembly determinants for a helical nucleocapsid with variable number of proteins per turn. Lobes protruding from alternate interfaces between each nucleoprotein are formed by the C-terminal domain of the nucleoprotein, together with viral proteins VP24 and VP35. Each nucleoprotein packages six RNA bases. The nucleocapsid interacts in an unusual, flexible "Velcro-like" manner with the viral matrix protein VP40. Determination of the structures of assembly intermediates showed that the nucleocapsid has a defined orientation during transport and budding. Together the data show striking architectural homology between the nucleocapsid helix of rhabdoviruses and filoviruses, but unexpected, fundamental differences in the mechanisms by which the nucleocapsids are then assembled together with matrix proteins and initiate membrane envelopment to release infectious virions, suggesting that the viruses have evolved different solutions to these conserved assembly steps.
format	article
author	Tanmay A M Bharat James D Riches Larissa Kolesnikova Sonja Welsch Verena Krähling Norman Davey Marie-Laure Parsy Stephan Becker John A G Briggs
author_facet	Tanmay A M Bharat James D Riches Larissa Kolesnikova Sonja Welsch Verena Krähling Norman Davey Marie-Laure Parsy Stephan Becker John A G Briggs
author_sort	Tanmay A M Bharat
title	Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.
title_short	Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.
title_full	Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.
title_fullStr	Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.
title_full_unstemmed	Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.
title_sort	cryo-electron tomography of marburg virus particles and their morphogenesis within infected cells.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/add284b5168b49b7a8f0d8b2547f688e
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Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.

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