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J Struct Biol. 2011 Apr;174(1):11-22. doi: 10.1016/j.jsb.2010.11.021. Epub 2010 Dec 3.

A structural analysis of M protein in coronavirus assembly and morphology.

Author information

1
School of Biological Sciences, University of Reading, RG6 6AJ, UK. b.w.neuman@reading.ac.uk

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.

PMID:
21130884
PMCID:
PMC4486061
DOI:
10.1016/j.jsb.2010.11.021
[Indexed for MEDLINE]
Free PMC Article

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