Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging

Abstract Ebola virus causes devastating hemorrhagic fever outbreaks for which no approved therapeutic exists. The viral nucleocapsid, which is minimally composed of the proteins NP, VP35, and VP24, represents an attractive target for drug development; however, the molecular determinants that govern...

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Autores principales:	Logan Banadyga, Thomas Hoenen, Xavier Ambroggio, Eric Dunham, Allison Groseth, Hideki Ebihara
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2bfc0c3ea9f142f7be19ae38b181ed11
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spelling	oai:doaj.org-article:2bfc0c3ea9f142f7be19ae38b181ed112021-12-02T11:40:23ZEbola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging10.1038/s41598-017-08167-82045-2322https://doaj.org/article/2bfc0c3ea9f142f7be19ae38b181ed112017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08167-8https://doaj.org/toc/2045-2322Abstract Ebola virus causes devastating hemorrhagic fever outbreaks for which no approved therapeutic exists. The viral nucleocapsid, which is minimally composed of the proteins NP, VP35, and VP24, represents an attractive target for drug development; however, the molecular determinants that govern the interactions and functions of these three proteins are still unknown. Through a series of mutational analyses, in combination with biochemical and bioinformatics approaches, we identified a region on VP24 that was critical for its interaction with NP. Importantly, we demonstrated that the interaction between VP24 and NP was required for both nucleocapsid assembly and genome packaging. Not only does this study underscore the critical role that these proteins play in the viral replication cycle, but it also identifies a key interaction interface on VP24 that may serve as a novel target for antiviral therapeutic intervention.Logan BanadygaThomas HoenenXavier AmbroggioEric DunhamAllison GrosethHideki EbiharaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Logan Banadyga Thomas Hoenen Xavier Ambroggio Eric Dunham Allison Groseth Hideki Ebihara Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging
description	Abstract Ebola virus causes devastating hemorrhagic fever outbreaks for which no approved therapeutic exists. The viral nucleocapsid, which is minimally composed of the proteins NP, VP35, and VP24, represents an attractive target for drug development; however, the molecular determinants that govern the interactions and functions of these three proteins are still unknown. Through a series of mutational analyses, in combination with biochemical and bioinformatics approaches, we identified a region on VP24 that was critical for its interaction with NP. Importantly, we demonstrated that the interaction between VP24 and NP was required for both nucleocapsid assembly and genome packaging. Not only does this study underscore the critical role that these proteins play in the viral replication cycle, but it also identifies a key interaction interface on VP24 that may serve as a novel target for antiviral therapeutic intervention.
format	article
author	Logan Banadyga Thomas Hoenen Xavier Ambroggio Eric Dunham Allison Groseth Hideki Ebihara
author_facet	Logan Banadyga Thomas Hoenen Xavier Ambroggio Eric Dunham Allison Groseth Hideki Ebihara
author_sort	Logan Banadyga
title	Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging
title_short	Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging
title_full	Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging
title_fullStr	Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging
title_full_unstemmed	Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging
title_sort	ebola virus vp24 interacts with np to facilitate nucleocapsid assembly and genome packaging
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/2bfc0c3ea9f142f7be19ae38b181ed11
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Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging

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