Abstract
The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.
Originalsprog | Engelsk |
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Tidsskrift | Journal of Structural Biology |
Vol/bind | 174 |
Udgave nummer | 1 |
Sider (fra-til) | 11-22 |
Antal sider | 12 |
ISSN | 1047-8477 |
DOI | |
Status | Udgivet - 1 apr. 2011 |