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-Structure paper
タイトル | Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM. |
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ジャーナル・号・ページ | PLoS Biol, Vol. 18, Issue 3, Page e3000649, Year 2020 |
掲載日 | 2020年3月31日 |
![]() | Joseph S Snowden / Daniel L Hurdiss / Oluwapelumi O Adeyemi / Neil A Ranson / Morgan R Herod / Nicola J Stonehouse / ![]() |
PubMed 要旨 | Icosahedral viral capsids must undergo conformational rearrangements to coordinate essential processes during the viral life cycle. Capturing such conformational flexibility has been technically ...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. |
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手法 | EM (単粒子) |
解像度 | 2.9 - 3.1 Å |
構造データ | EMDB-10103, PDB-6s6l: ![]() EMDB-10127: ![]() EMDB-10128: |
由来 |
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![]() | VIRUS / Norovirus / Capsid / VP1 |