dc.contributor.author |
Jaballah, SA |
en |
dc.contributor.author |
Bailey, GD |
en |
dc.contributor.author |
Desfosses, A |
en |
dc.contributor.author |
Hyun, J |
en |
dc.contributor.author |
Mitra, Alok |
en |
dc.contributor.author |
Kingston, Richard |
en |
dc.date.accessioned |
2017-10-17T02:15:07Z |
en |
dc.date.issued |
2017-06-06 |
en |
dc.identifier.citation |
Scientific Reports 7(1):2913 06 Jun 2017 |
en |
dc.identifier.issn |
2045-2322 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/36114 |
en |
dc.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. |
en |
dc.format.medium |
Electronic |
en |
dc.language |
eng |
en |
dc.publisher |
Nature Publishing Group |
en |
dc.relation.ispartofseries |
Scientific Reports |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/2045-2322/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
en |
dc.title |
In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1038/s41598-017-02060-0 |
en |
pubs.issue |
1 |
en |
pubs.volume |
7 |
en |
dc.description.version |
VoR - Version of Record |
en |
dc.rights.holder |
Copyright: The authors |
en |
dc.identifier.pmid |
28588198 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
629219 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
2045-2322 |
en |
pubs.number |
2913 |
en |
pubs.record-created-at-source-date |
2017-10-17 |
en |
pubs.dimensions-id |
28588198 |
en |