In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature

Abstract During a proteolytically-driven maturation process, the orthoretroviral capsid protein (CA) assembles to form the convex shell that surrounds the viral genome. In some orthoretroviruses, including Rous Sarcoma Virus (RSV), CA carries a short and hydrophobic spacer peptide (SP) at its C-term...

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Autores principales:	Soumeya A. Jaballah, Graham D. Bailey, Ambroise Desfosses, Jaekyung Hyun, Alok K. Mitra, Richard L. Kingston
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/736ac435609a475eba12d9102ea5d11c
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spelling	oai:doaj.org-article:736ac435609a475eba12d9102ea5d11c2021-12-02T15:06:17ZIn vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature10.1038/s41598-017-02060-02045-2322https://doaj.org/article/736ac435609a475eba12d9102ea5d11c2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02060-0https://doaj.org/toc/2045-2322Abstract During a proteolytically-driven maturation process, the orthoretroviral capsid protein (CA) assembles to form the convex shell that surrounds the viral genome. In some orthoretroviruses, including Rous Sarcoma Virus (RSV), CA carries a short and hydrophobic spacer peptide (SP) at its C-terminus early in the maturation process, which is progressively removed as maturation proceeds. In this work, we show that RSV CA assembles in vitro at near-physiological temperatures, forming hexamer tubes that effectively model the mature capsid surface. Tube assembly is strongly influenced by electrostatic effects, and is a nucleated process that remains thermodynamically favored at lower temperatures, but is effectively arrested by the large Gibbs energy barrier associated with nucleation. RSV CA tubes are multi-layered, being formed by nested and concentric tubes of capsid hexamers. However the spacer peptide acts as a layering determinant during tube assembly. If only a minor fraction of CA-SP is present, multi-layered tube formation is blocked, and single-layered tubes predominate. This likely prevents formation of biologically aberrant multi-layered capsids in the virion. The generation of single-layered hexamer tubes facilitated 3D helical image reconstruction from cryo-electron microscopy data, revealing the basic tube architecture.Soumeya A. JaballahGraham D. BaileyAmbroise DesfossesJaekyung HyunAlok K. MitraRichard L. KingstonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-17 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Soumeya A. Jaballah Graham D. Bailey Ambroise Desfosses Jaekyung Hyun Alok K. Mitra Richard L. Kingston In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
description	Abstract During a proteolytically-driven maturation process, the orthoretroviral capsid protein (CA) assembles to form the convex shell that surrounds the viral genome. In some orthoretroviruses, including Rous Sarcoma Virus (RSV), CA carries a short and hydrophobic spacer peptide (SP) at its C-terminus early in the maturation process, which is progressively removed as maturation proceeds. In this work, we show that RSV CA assembles in vitro at near-physiological temperatures, forming hexamer tubes that effectively model the mature capsid surface. Tube assembly is strongly influenced by electrostatic effects, and is a nucleated process that remains thermodynamically favored at lower temperatures, but is effectively arrested by the large Gibbs energy barrier associated with nucleation. RSV CA tubes are multi-layered, being formed by nested and concentric tubes of capsid hexamers. However the spacer peptide acts as a layering determinant during tube assembly. If only a minor fraction of CA-SP is present, multi-layered tube formation is blocked, and single-layered tubes predominate. This likely prevents formation of biologically aberrant multi-layered capsids in the virion. The generation of single-layered hexamer tubes facilitated 3D helical image reconstruction from cryo-electron microscopy data, revealing the basic tube architecture.
format	article
author	Soumeya A. Jaballah Graham D. Bailey Ambroise Desfosses Jaekyung Hyun Alok K. Mitra Richard L. Kingston
author_facet	Soumeya A. Jaballah Graham D. Bailey Ambroise Desfosses Jaekyung Hyun Alok K. Mitra Richard L. Kingston
author_sort	Soumeya A. Jaballah
title	In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
title_short	In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
title_full	In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
title_fullStr	In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
title_full_unstemmed	In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
title_sort	in vitro assembly of the rous sarcoma virus capsid protein into hexamer tubes at physiological temperature
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/736ac435609a475eba12d9102ea5d11c
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In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature

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