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A Structural analysis of M protein in coronavirus assembly and morphology

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Benjamin W. Neuman
  • Gabriella Kiss
  • Andreas H. Kunding
  • David Bhella
  • M. Fazil Baksh
  • Stephen Connelly
  • Ben Droese
  • Joseph P. Klaus
  • Shinji Makino
  • Stanley G. Sawicji
  • Stuart G. Siddell
  • Stamou, Dimitrios
  • Ian A. Wilson
  • Peter Kuhn
  • Michael J. Buchmeier
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.
OriginalsprogEngelsk
TidsskriftJournal of Structural Biology
Vol/bind174
Udgave nummer1
Sider (fra-til)11-22
Antal sider12
ISSN1047-8477
DOI
StatusUdgivet - 1 apr. 2011

ID: 33901052