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.
Original language | English (US) |
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Pages (from-to) | 11-22 |
Number of pages | 12 |
Journal | Journal of Structural Biology |
Volume | 174 |
Issue number | 1 |
DOIs | |
State | Published - Apr 2011 |
Keywords
- Coronavirus
- Cryo-electron microscopy
- Cryo-electron tomography
- Pleomorphic virus structure
- Viral matrix protein
ASJC Scopus subject areas
- Structural Biology