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Virus assembly, allostery and antivirals

Assembly of virus capsids and surface proteins must be regulated to ensure that the resulting complex is an infectious virion. In this review, we examine assembly of virus capsids, focusing on hepatitis B virus and bacteriophage MS2, and formation of glycoproteins in the alphaviruses. These systems...

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Detalles Bibliográficos
Autores principales: Zlotnick, Adam, Mukhopadhyay, Suchetana
Formato: Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3026312/
https://www.ncbi.nlm.nih.gov/pubmed/21163649
http://dx.doi.org/10.1016/j.tim.2010.11.003
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author Zlotnick, Adam
Mukhopadhyay, Suchetana
author_facet Zlotnick, Adam
Mukhopadhyay, Suchetana
author_sort Zlotnick, Adam
collection PubMed
description Assembly of virus capsids and surface proteins must be regulated to ensure that the resulting complex is an infectious virion. In this review, we examine assembly of virus capsids, focusing on hepatitis B virus and bacteriophage MS2, and formation of glycoproteins in the alphaviruses. These systems are structurally and biochemically well-characterized and are simplest-case paradigms of self-assembly. Published data suggest that capsid and glycoprotein assembly is subject to allosteric regulation, that is regulation at the level of conformational change. The hypothesis that allostery is a common theme in viruses suggests that deregulation of capsid and glycoprotein assembly by small molecule effectors will be an attractive antiviral strategy, as has been demonstrated with hepatitis B virus.
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spelling pubmed-30263122012-01-01 Virus assembly, allostery and antivirals Zlotnick, Adam Mukhopadhyay, Suchetana Trends Microbiol Article Assembly of virus capsids and surface proteins must be regulated to ensure that the resulting complex is an infectious virion. In this review, we examine assembly of virus capsids, focusing on hepatitis B virus and bacteriophage MS2, and formation of glycoproteins in the alphaviruses. These systems are structurally and biochemically well-characterized and are simplest-case paradigms of self-assembly. Published data suggest that capsid and glycoprotein assembly is subject to allosteric regulation, that is regulation at the level of conformational change. The hypothesis that allostery is a common theme in viruses suggests that deregulation of capsid and glycoprotein assembly by small molecule effectors will be an attractive antiviral strategy, as has been demonstrated with hepatitis B virus. Elsevier Ltd. 2011-01 2010-12-14 /pmc/articles/PMC3026312/ /pubmed/21163649 http://dx.doi.org/10.1016/j.tim.2010.11.003 Text en Copyright © 2010 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Zlotnick, Adam
Mukhopadhyay, Suchetana
Virus assembly, allostery and antivirals
title Virus assembly, allostery and antivirals
title_full Virus assembly, allostery and antivirals
title_fullStr Virus assembly, allostery and antivirals
title_full_unstemmed Virus assembly, allostery and antivirals
title_short Virus assembly, allostery and antivirals
title_sort virus assembly, allostery and antivirals
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3026312/
https://www.ncbi.nlm.nih.gov/pubmed/21163649
http://dx.doi.org/10.1016/j.tim.2010.11.003
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