Tsg101 chaperone function revealed by HIV-1 assembly inhibitors

Tsg101 is a component of the host cellular ESCRT machinery and is required for HIV-1 replication. Here, the authors show that disruption of ubiquitin binding of the Tsg101 UEV domain through commonly used drugs arrests virus assembly, which might facilitate the development of potent HIV inhibitors.

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Autores principales:	Madeleine Strickland, Lorna S. Ehrlich, Susan Watanabe, Mahfuz Khan, Marie-Paule Strub, Chi-Hao Luan, Michael D. Powell, Jonathan Leis, Nico Tjandra, Carol A. Carter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2ecc918c7b1b4a77b36ae1b966756894
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spelling	oai:doaj.org-article:2ecc918c7b1b4a77b36ae1b9667568942021-12-02T14:41:07ZTsg101 chaperone function revealed by HIV-1 assembly inhibitors10.1038/s41467-017-01426-22041-1723https://doaj.org/article/2ecc918c7b1b4a77b36ae1b9667568942017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01426-2https://doaj.org/toc/2041-1723Tsg101 is a component of the host cellular ESCRT machinery and is required for HIV-1 replication. Here, the authors show that disruption of ubiquitin binding of the Tsg101 UEV domain through commonly used drugs arrests virus assembly, which might facilitate the development of potent HIV inhibitors.Madeleine StricklandLorna S. EhrlichSusan WatanabeMahfuz KhanMarie-Paule StrubChi-Hao LuanMichael D. PowellJonathan LeisNico TjandraCarol A. CarterNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Madeleine Strickland Lorna S. Ehrlich Susan Watanabe Mahfuz Khan Marie-Paule Strub Chi-Hao Luan Michael D. Powell Jonathan Leis Nico Tjandra Carol A. Carter Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
description	Tsg101 is a component of the host cellular ESCRT machinery and is required for HIV-1 replication. Here, the authors show that disruption of ubiquitin binding of the Tsg101 UEV domain through commonly used drugs arrests virus assembly, which might facilitate the development of potent HIV inhibitors.
format	article
author	Madeleine Strickland Lorna S. Ehrlich Susan Watanabe Mahfuz Khan Marie-Paule Strub Chi-Hao Luan Michael D. Powell Jonathan Leis Nico Tjandra Carol A. Carter
author_facet	Madeleine Strickland Lorna S. Ehrlich Susan Watanabe Mahfuz Khan Marie-Paule Strub Chi-Hao Luan Michael D. Powell Jonathan Leis Nico Tjandra Carol A. Carter
author_sort	Madeleine Strickland
title	Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
title_short	Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
title_full	Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
title_fullStr	Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
title_full_unstemmed	Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
title_sort	tsg101 chaperone function revealed by hiv-1 assembly inhibitors
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/2ecc918c7b1b4a77b36ae1b966756894
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Tsg101 chaperone function revealed by HIV-1 assembly inhibitors

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