Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.

The genus Orthobunyavirus within the family Bunyaviridae constitutes an expanding group of emerging viruses, which threaten human and animal health. Despite the medical importance, little is known about orthobunyavirus structure, a prerequisite for understanding virus assembly and entry. Here, using...

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Autores principales:	Thomas A Bowden, David Bitto, Angela McLees, Christelle Yeromonahos, Richard M Elliott, Juha T Huiskonen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/e9f93a65ccf540128d40037714277cd7
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spelling	oai:doaj.org-article:e9f93a65ccf540128d40037714277cd72021-11-18T06:05:37ZOrthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.1553-73661553-737410.1371/journal.ppat.1003374https://doaj.org/article/e9f93a65ccf540128d40037714277cd72013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23696739/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The genus Orthobunyavirus within the family Bunyaviridae constitutes an expanding group of emerging viruses, which threaten human and animal health. Despite the medical importance, little is known about orthobunyavirus structure, a prerequisite for understanding virus assembly and entry. Here, using electron cryo-tomography, we report the ultrastructure of Bunyamwera virus, the prototypic member of this genus. Whilst Bunyamwera virions are pleomorphic in shape, they display a locally ordered lattice of glycoprotein spikes. Each spike protrudes 18 nm from the viral membrane and becomes disordered upon introduction to an acidic environment. Using sub-tomogram averaging, we derived a three-dimensional model of the trimeric pre-fusion glycoprotein spike to 3-nm resolution. The glycoprotein spike consists mainly of the putative class-II fusion glycoprotein and exhibits a unique tripod-like arrangement. Protein-protein contacts between neighbouring spikes occur at membrane-proximal regions and intra-spike contacts at membrane-distal regions. This trimeric assembly deviates from previously observed fusion glycoprotein arrangements, suggesting a greater than anticipated repertoire of viral fusion glycoprotein oligomerization. Our study provides evidence of a pH-dependent conformational change that occurs during orthobunyaviral entry into host cells and a blueprint for the structure of this group of emerging pathogens.Thomas A BowdenDavid BittoAngela McLeesChristelle YeromonahosRichard M ElliottJuha T HuiskonenPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 5, p e1003374 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Thomas A Bowden David Bitto Angela McLees Christelle Yeromonahos Richard M Elliott Juha T Huiskonen Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
description	The genus Orthobunyavirus within the family Bunyaviridae constitutes an expanding group of emerging viruses, which threaten human and animal health. Despite the medical importance, little is known about orthobunyavirus structure, a prerequisite for understanding virus assembly and entry. Here, using electron cryo-tomography, we report the ultrastructure of Bunyamwera virus, the prototypic member of this genus. Whilst Bunyamwera virions are pleomorphic in shape, they display a locally ordered lattice of glycoprotein spikes. Each spike protrudes 18 nm from the viral membrane and becomes disordered upon introduction to an acidic environment. Using sub-tomogram averaging, we derived a three-dimensional model of the trimeric pre-fusion glycoprotein spike to 3-nm resolution. The glycoprotein spike consists mainly of the putative class-II fusion glycoprotein and exhibits a unique tripod-like arrangement. Protein-protein contacts between neighbouring spikes occur at membrane-proximal regions and intra-spike contacts at membrane-distal regions. This trimeric assembly deviates from previously observed fusion glycoprotein arrangements, suggesting a greater than anticipated repertoire of viral fusion glycoprotein oligomerization. Our study provides evidence of a pH-dependent conformational change that occurs during orthobunyaviral entry into host cells and a blueprint for the structure of this group of emerging pathogens.
format	article
author	Thomas A Bowden David Bitto Angela McLees Christelle Yeromonahos Richard M Elliott Juha T Huiskonen
author_facet	Thomas A Bowden David Bitto Angela McLees Christelle Yeromonahos Richard M Elliott Juha T Huiskonen
author_sort	Thomas A Bowden
title	Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
title_short	Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
title_full	Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
title_fullStr	Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
title_full_unstemmed	Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
title_sort	orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e9f93a65ccf540128d40037714277cd7
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Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike.

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