Allosteric conformational changes of human HBV core protein transform its assembly

Abstract Hepatitis B Virus core protein (HBc) has multiple roles in the viral lifecycle: viral assembly, compartment for reverse transcription, intracellular trafficking, and nuclear functions. HBc displays assembly polymorphism - it can assemble into icosahedral capsid and aberrant non-capsid struc...

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Autores principales:	Chuang Liu, Guizhen Fan, Zhao Wang, Hong-Song Chen, Chang-Cheng Yin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ddc1888260914bea9de0fc52e2d7833e
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spelling	oai:doaj.org-article:ddc1888260914bea9de0fc52e2d7833e2021-12-02T11:52:44ZAllosteric conformational changes of human HBV core protein transform its assembly10.1038/s41598-017-01568-92045-2322https://doaj.org/article/ddc1888260914bea9de0fc52e2d7833e2017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01568-9https://doaj.org/toc/2045-2322Abstract Hepatitis B Virus core protein (HBc) has multiple roles in the viral lifecycle: viral assembly, compartment for reverse transcription, intracellular trafficking, and nuclear functions. HBc displays assembly polymorphism - it can assemble into icosahedral capsid and aberrant non-capsid structures. It has been hypothesized that the assembly polymorphism is due to allosteric conformational changes of HBc dimer, the smallest assembly unit, however, the mechanism governing the polymorphic assembly of the HBc dimer is still elusive. By using the experimental antiviral drug BAY 41-4109, we successfully transformed the HBc assembly from icosahedral capsid to helical tube. Structural analyses of HBc dimers from helical tubes, T = 4 icosahedral capsid, and sheet-like HBc ensemble revealed differences within the inter-dimer interface. Disruption of the HBc inter-dimer interface may likely promote the various assembly forms of HBc. Our work provides new structural insights into the HBV assembly mechanism and strategic guide for anti-HBV drug design.Chuang LiuGuizhen FanZhao WangHong-Song ChenChang-Cheng YinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chuang Liu Guizhen Fan Zhao Wang Hong-Song Chen Chang-Cheng Yin Allosteric conformational changes of human HBV core protein transform its assembly
description	Abstract Hepatitis B Virus core protein (HBc) has multiple roles in the viral lifecycle: viral assembly, compartment for reverse transcription, intracellular trafficking, and nuclear functions. HBc displays assembly polymorphism - it can assemble into icosahedral capsid and aberrant non-capsid structures. It has been hypothesized that the assembly polymorphism is due to allosteric conformational changes of HBc dimer, the smallest assembly unit, however, the mechanism governing the polymorphic assembly of the HBc dimer is still elusive. By using the experimental antiviral drug BAY 41-4109, we successfully transformed the HBc assembly from icosahedral capsid to helical tube. Structural analyses of HBc dimers from helical tubes, T = 4 icosahedral capsid, and sheet-like HBc ensemble revealed differences within the inter-dimer interface. Disruption of the HBc inter-dimer interface may likely promote the various assembly forms of HBc. Our work provides new structural insights into the HBV assembly mechanism and strategic guide for anti-HBV drug design.
format	article
author	Chuang Liu Guizhen Fan Zhao Wang Hong-Song Chen Chang-Cheng Yin
author_facet	Chuang Liu Guizhen Fan Zhao Wang Hong-Song Chen Chang-Cheng Yin
author_sort	Chuang Liu
title	Allosteric conformational changes of human HBV core protein transform its assembly
title_short	Allosteric conformational changes of human HBV core protein transform its assembly
title_full	Allosteric conformational changes of human HBV core protein transform its assembly
title_fullStr	Allosteric conformational changes of human HBV core protein transform its assembly
title_full_unstemmed	Allosteric conformational changes of human HBV core protein transform its assembly
title_sort	allosteric conformational changes of human hbv core protein transform its assembly
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ddc1888260914bea9de0fc52e2d7833e
work_keys_str_mv	AT chuangliu allostericconformationalchangesofhumanhbvcoreproteintransformitsassembly AT guizhenfan allostericconformationalchangesofhumanhbvcoreproteintransformitsassembly AT zhaowang allostericconformationalchangesofhumanhbvcoreproteintransformitsassembly AT hongsongchen allostericconformationalchangesofhumanhbvcoreproteintransformitsassembly AT changchengyin allostericconformationalchangesofhumanhbvcoreproteintransformitsassembly
_version_	1718394956864815104

Allosteric conformational changes of human HBV core protein transform its assembly

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