A structural analysis of M protein in coronavirus assembly and morphology
Neuman, B. W., Kiss, G., Kunding, A. H., Bhella, D., Baksh, M. F., Connelly, S., Droese, B., Klaus, J. P., Makino, S., Sawicki, S. G., Siddell, S. G., Stamou, D. G., Wilson, I. A., Kuhn, P. and Buchmeier, M. J. (2011) A structural analysis of M protein in coronavirus assembly and morphology. Journal of Structural Biology, 174 (1). pp. 11-22. ISSN 1047-8477
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To link to this article DOI: 10.1016/j.jsb.2010.11.021
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.