Hurdiss, DL, Morgan, EL, Thompson, RF et al. (4 more authors) (2016) New Structural Insights into the Genome and Minor Capsid Proteins of BK Polyomavirus using Cryo-Electron Microscopy. Structure, 24 (4). pp. 528-536. ISSN 0969-2126
Abstract
BK polyomavirus is the causative agent of several diseases in transplant patients and the immunosuppressed. In order to better understand the structure and life cycle of BK, we produced infectious virions and VP1-only virus-like particles in cell culture, and determined their three-dimensional structures using cryo-electron microscopy (EM) and single-particle image processing. The resulting 7.6-Å resolution structure of BK and 9.1-Å resolution of the virus-like particles are the highest-resolution cryo-EM structures of any polyomavirus. These structures confirm that the architecture of the major structural protein components of these human polyomaviruses are similar to previous structures from other hosts, but give new insight into the location and role of the enigmatic minor structural proteins, VP2 and VP3. We also observe two shells of electron density, which we attribute to a structurally ordered part of the viral genome, and discrete contacts between this density and both VP1 and the minor capsid proteins.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Funding Information: | Funder Grant number Wellcome Trust 090932/Z/09/Z Wellcome Trust 094232/Z/10/Z MRC MR/K012665/1 Kidney Research Fund UK RP25/2013 |
Depositing User: | Symplectic Publications |
Date Deposited: | 10 Feb 2016 10:48 |
Last Modified: | 12 Feb 2019 11:55 |
Published Version: | http://dx.doi.org/10.1016/j.str.2016.02.008 |
Status: | Published |
Publisher: | Elsevier (Cell Press) |
Identification Number: | 10.1016/j.str.2016.02.008 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:94878 |