Structural studies of the giant mimivirus.

Mimivirus is the largest known virus whose genome and physical size are comparable to some small bacteria, blurring the boundary between a virus and a cell. Structural studies of Mimivirus have been difficult because of its size and long surface fibers. Here we report the use of enzymatic digestions...

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Autores principales:	Chuan Xiao, Yurii G Kuznetsov, Siyang Sun, Susan L Hafenstein, Victor A Kostyuchenko, Paul R Chipman, Marie Suzan-Monti, Didier Raoult, Alexander McPherson, Michael G Rossmann
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/e4761cd9d7c34ca48f50e686e1dd403e
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spelling	oai:doaj.org-article:e4761cd9d7c34ca48f50e686e1dd403e2021-11-25T05:34:12ZStructural studies of the giant mimivirus.1544-91731545-788510.1371/journal.pbio.1000092https://doaj.org/article/e4761cd9d7c34ca48f50e686e1dd403e2009-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19402750/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Mimivirus is the largest known virus whose genome and physical size are comparable to some small bacteria, blurring the boundary between a virus and a cell. Structural studies of Mimivirus have been difficult because of its size and long surface fibers. Here we report the use of enzymatic digestions to remove the surface fibers of Mimivirus in order to expose the surface of the viral capsid. Cryo-electron microscopy (cryoEM) and atomic force microscopy were able to show that the 20 icosahedral faces of Mimivirus capsids have hexagonal arrays of depressions. Each depression is surrounded by six trimeric capsomers that are similar in structure to those in many other large, icosahedral double-stranded DNA viruses. Whereas in most viruses these capsomers are hexagonally close-packed with the same orientation in each face, in Mimivirus there are vacancies at the systematic depressions with neighboring capsomers differing in orientation by 60 degrees . The previously observed starfish-shaped feature is well-resolved and found to be on each virus particle and is associated with a special pentameric vertex. The arms of the starfish fit into the gaps between the five faces surrounding the unique vertex, acting as a seal. Furthermore, the enveloped nucleocapsid is accurately positioned and oriented within the capsid with a concave surface facing the unique vertex. Thus, the starfish-shaped feature and the organization of the nucleocapsid might regulate the delivery of the genome to the host. The structure of Mimivirus, as well as the various fiber components observed in the virus, suggests that the Mimivirus genome includes genes derived from both eukaryotic and prokaryotic organisms. The three-dimensional cryoEM reconstruction reported here is of a virus with a volume that is one order of magnitude larger than any previously reported molecular assembly studied at a resolution of equal to or better than 65 Angstroms.Chuan XiaoYurii G KuznetsovSiyang SunSusan L HafensteinVictor A KostyuchenkoPaul R ChipmanMarie Suzan-MontiDidier RaoultAlexander McPhersonMichael G RossmannPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 7, Iss 4, p e92 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Chuan Xiao Yurii G Kuznetsov Siyang Sun Susan L Hafenstein Victor A Kostyuchenko Paul R Chipman Marie Suzan-Monti Didier Raoult Alexander McPherson Michael G Rossmann Structural studies of the giant mimivirus.
description	Mimivirus is the largest known virus whose genome and physical size are comparable to some small bacteria, blurring the boundary between a virus and a cell. Structural studies of Mimivirus have been difficult because of its size and long surface fibers. Here we report the use of enzymatic digestions to remove the surface fibers of Mimivirus in order to expose the surface of the viral capsid. Cryo-electron microscopy (cryoEM) and atomic force microscopy were able to show that the 20 icosahedral faces of Mimivirus capsids have hexagonal arrays of depressions. Each depression is surrounded by six trimeric capsomers that are similar in structure to those in many other large, icosahedral double-stranded DNA viruses. Whereas in most viruses these capsomers are hexagonally close-packed with the same orientation in each face, in Mimivirus there are vacancies at the systematic depressions with neighboring capsomers differing in orientation by 60 degrees . The previously observed starfish-shaped feature is well-resolved and found to be on each virus particle and is associated with a special pentameric vertex. The arms of the starfish fit into the gaps between the five faces surrounding the unique vertex, acting as a seal. Furthermore, the enveloped nucleocapsid is accurately positioned and oriented within the capsid with a concave surface facing the unique vertex. Thus, the starfish-shaped feature and the organization of the nucleocapsid might regulate the delivery of the genome to the host. The structure of Mimivirus, as well as the various fiber components observed in the virus, suggests that the Mimivirus genome includes genes derived from both eukaryotic and prokaryotic organisms. The three-dimensional cryoEM reconstruction reported here is of a virus with a volume that is one order of magnitude larger than any previously reported molecular assembly studied at a resolution of equal to or better than 65 Angstroms.
format	article
author	Chuan Xiao Yurii G Kuznetsov Siyang Sun Susan L Hafenstein Victor A Kostyuchenko Paul R Chipman Marie Suzan-Monti Didier Raoult Alexander McPherson Michael G Rossmann
author_facet	Chuan Xiao Yurii G Kuznetsov Siyang Sun Susan L Hafenstein Victor A Kostyuchenko Paul R Chipman Marie Suzan-Monti Didier Raoult Alexander McPherson Michael G Rossmann
author_sort	Chuan Xiao
title	Structural studies of the giant mimivirus.
title_short	Structural studies of the giant mimivirus.
title_full	Structural studies of the giant mimivirus.
title_fullStr	Structural studies of the giant mimivirus.
title_full_unstemmed	Structural studies of the giant mimivirus.
title_sort	structural studies of the giant mimivirus.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/e4761cd9d7c34ca48f50e686e1dd403e
work_keys_str_mv	AT chuanxiao structuralstudiesofthegiantmimivirus AT yuriigkuznetsov structuralstudiesofthegiantmimivirus AT siyangsun structuralstudiesofthegiantmimivirus AT susanlhafenstein structuralstudiesofthegiantmimivirus AT victorakostyuchenko structuralstudiesofthegiantmimivirus AT paulrchipman structuralstudiesofthegiantmimivirus AT mariesuzanmonti structuralstudiesofthegiantmimivirus AT didierraoult structuralstudiesofthegiantmimivirus AT alexandermcpherson structuralstudiesofthegiantmimivirus AT michaelgrossmann structuralstudiesofthegiantmimivirus
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Structural studies of the giant mimivirus.

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