Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses

Abstract Whereas the protein composition and overall shape of several giant virus capsids have been described, the mechanism by which these large capsids assemble remains enigmatic. Here, we present a reconstruction of the capsid of Cafeteria roenbergensis virus (CroV), one of the largest viruses an...

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Autores principales:	Chuan Xiao, Matthias G. Fischer, Duer M. Bolotaulo, Nancy Ulloa-Rondeau, Gustavo A. Avila, Curtis A. Suttle
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ec5bbca9372d498daf6956b788609806
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spelling	oai:doaj.org-article:ec5bbca9372d498daf6956b7886098062021-12-02T12:31:48ZCryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses10.1038/s41598-017-05824-w2045-2322https://doaj.org/article/ec5bbca9372d498daf6956b7886098062017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05824-whttps://doaj.org/toc/2045-2322Abstract Whereas the protein composition and overall shape of several giant virus capsids have been described, the mechanism by which these large capsids assemble remains enigmatic. Here, we present a reconstruction of the capsid of Cafeteria roenbergensis virus (CroV), one of the largest viruses analyzed by cryo-electron microscopy (cryo-EM) to date. The CroV capsid has a diameter of 3,000 Å and a Triangulation number of 499. Unlike related mimiviruses, the CroV capsid is not decorated with glycosylated surface fibers, but features 30 Å-long surface protrusions that are formed by loops of the major capsid protein. Based on the orientation of capsomers in the cryo-EM reconstruction, we propose that the capsids of CroV and related giant viruses are assembled by a newly conceived assembly pathway that initiates at a five-fold vertex and continuously proceeds outwards in a spiraling fashion.Chuan XiaoMatthias G. FischerDuer M. BolotauloNancy Ulloa-RondeauGustavo A. AvilaCurtis A. SuttleNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chuan Xiao Matthias G. Fischer Duer M. Bolotaulo Nancy Ulloa-Rondeau Gustavo A. Avila Curtis A. Suttle Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
description	Abstract Whereas the protein composition and overall shape of several giant virus capsids have been described, the mechanism by which these large capsids assemble remains enigmatic. Here, we present a reconstruction of the capsid of Cafeteria roenbergensis virus (CroV), one of the largest viruses analyzed by cryo-electron microscopy (cryo-EM) to date. The CroV capsid has a diameter of 3,000 Å and a Triangulation number of 499. Unlike related mimiviruses, the CroV capsid is not decorated with glycosylated surface fibers, but features 30 Å-long surface protrusions that are formed by loops of the major capsid protein. Based on the orientation of capsomers in the cryo-EM reconstruction, we propose that the capsids of CroV and related giant viruses are assembled by a newly conceived assembly pathway that initiates at a five-fold vertex and continuously proceeds outwards in a spiraling fashion.
format	article
author	Chuan Xiao Matthias G. Fischer Duer M. Bolotaulo Nancy Ulloa-Rondeau Gustavo A. Avila Curtis A. Suttle
author_facet	Chuan Xiao Matthias G. Fischer Duer M. Bolotaulo Nancy Ulloa-Rondeau Gustavo A. Avila Curtis A. Suttle
author_sort	Chuan Xiao
title	Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
title_short	Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
title_full	Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
title_fullStr	Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
title_full_unstemmed	Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
title_sort	cryo-em reconstruction of the cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ec5bbca9372d498daf6956b788609806
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Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses

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