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

A structural analysis of M protein in coronavirus assembly and morphology.
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DOI:
10.1016/j.jsb.2010.11.021
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发表时间:
2011-04
影响因子:
3
通讯作者:
Buchmeier, Michaell J.
Buchmeier, Michaell J.
中科院分区:
生物学3区
文献类型:
--
作者:
Neuman, Benjamin W.;Kiss, Gabriella;Kunding, Andreas H.;Bhella, David;Baksh, M. Fazil;Connelly, Stephen;Droese, Ben;Klaus, Joseph P.;Makino, Shinji;Sawicki, Stanley G.;Siddell, Stuart G.;Stamou, Dimitrios G.;Wilson, Ian A.;Kuhn, Peter;Buchmeier, Michaell J.

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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.
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