IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating

The mechanisms that drive formation of the HIV capsid, first as an immature particle and then as a mature protein shell, remain incompletely understood. Recent discoveries of positively-charged rings in the immature and mature protein hexamer subunits that comprise them and their binding to the cell...

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Detalles Bibliográficos
Autores principales: Dick, Robert A., Mallery, Donna L., Vogt, Volker M., James, Leo C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6267275/
https://www.ncbi.nlm.nih.gov/pubmed/30445742
http://dx.doi.org/10.3390/v10110640
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author Dick, Robert A.
Mallery, Donna L.
Vogt, Volker M.
James, Leo C.
author_facet Dick, Robert A.
Mallery, Donna L.
Vogt, Volker M.
James, Leo C.
author_sort Dick, Robert A.
collection PubMed
description The mechanisms that drive formation of the HIV capsid, first as an immature particle and then as a mature protein shell, remain incompletely understood. Recent discoveries of positively-charged rings in the immature and mature protein hexamer subunits that comprise them and their binding to the cellular metabolite inositol hexakisphosphate (IP6) have stimulated exciting new hypotheses. In this paper, we discuss how data from multiple structural and biochemical approaches are revealing potential roles for IP6 in the HIV-1 replication cycle from assembly to uncoating.
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spelling pubmed-62672752018-12-07 IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating Dick, Robert A. Mallery, Donna L. Vogt, Volker M. James, Leo C. Viruses Review The mechanisms that drive formation of the HIV capsid, first as an immature particle and then as a mature protein shell, remain incompletely understood. Recent discoveries of positively-charged rings in the immature and mature protein hexamer subunits that comprise them and their binding to the cellular metabolite inositol hexakisphosphate (IP6) have stimulated exciting new hypotheses. In this paper, we discuss how data from multiple structural and biochemical approaches are revealing potential roles for IP6 in the HIV-1 replication cycle from assembly to uncoating. MDPI 2018-11-15 /pmc/articles/PMC6267275/ /pubmed/30445742 http://dx.doi.org/10.3390/v10110640 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Dick, Robert A.
Mallery, Donna L.
Vogt, Volker M.
James, Leo C.
IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
title IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
title_full IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
title_fullStr IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
title_full_unstemmed IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
title_short IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
title_sort ip6 regulation of hiv capsid assembly, stability, and uncoating
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6267275/
https://www.ncbi.nlm.nih.gov/pubmed/30445742
http://dx.doi.org/10.3390/v10110640
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