A structural analysis of M protein in coronavirus assembly and morphology

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

来源：Journal of Structural Biology, 2011, 174(1): 11-22.

DOI：10.1016/j.jsb.2010.11.021

• Cryo-electron microscopy
• Cryo-electron tomography
• Pleomorphic virus structure
• Coronavirus
• Viral matrix protein

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.

• 出版日期2011-4