EMD-10127

Single-particle
2.9 Å
EMD-10127 Deposition: 16/07/2019
Map released: 27/05/2020
Last modified: 27/05/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10127

Thermally-inactivated murine norovirus (MNV-1)

EMD-10127

Single-particle
2.9 Å
EMD-10127 Deposition: 16/07/2019
Map released: 27/05/2020
Last modified: 27/05/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Murine norovirus 1
Sample: Murine norovirus 1

Deposition Authors: Snowden JS, Hurdiss DL, Adeyemi OO, Ranson NA, Herod MR, Stonehouse NJ
Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM.
Snowden JS , Hurdiss DL , Adeyemi OO , Ranson NA , Herod MR , Stonehouse NJ
(2020) PLoS Biol , 18 , e3000649 - e3000649
PUBMED: 32231352
DOI: doi:10.1371/journal.pbio.3000649
ISSN: 1545-7885
Abstract:
Icosahedral viral capsids must undergo conformational rearrangements to coordinate essential processes during the viral life cycle. Capturing such conformational flexibility has been technically challenging yet could be key for developing rational therapeutic agents to combat infections. Noroviruses are nonenveloped, icosahedral viruses of global importance to human health. They are a common cause of acute gastroenteritis, yet no vaccines or specific antiviral agents are available. Here, we use genetics and cryo-electron microscopy (cryo-EM) to study the high-resolution solution structures of murine norovirus as a model for human viruses. By comparing our 3 structures (at 2.9- to 3.1-Å resolution), we show that whilst there is little change to the shell domain of the capsid, the radiating protruding domains are flexible, adopting distinct states both independently and synchronously. In doing so, the capsids sample a range of conformational space, with implications for maintaining virion stability and infectivity.