Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 174, Issue 1, Pages 11-22Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2010.11.021
Keywords
Cryo-electron microscopy; Cryo-electron tomography; Pleomorphic virus structure; Coronavirus; Viral matrix protein
Funding
- NIH/NIAID [HHSN-266200400058C, AI-059799, AI-25913, AI-29984, AI-72493]
- Danish Research Council
- National Institutes of Health though the National Center for Research Resources' [RR17573]
- Medical Research Council [MC_UP_A550_1029] Funding Source: researchfish
- MRC [MC_UP_A550_1029] Funding Source: UKRI
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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. (C) 2010 Elsevier Inc. All rights reserved.
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