A structural analysis of M protein in coronavirus assembly and morphology

Publication: Research - peer-reviewJournal article – Annual report year: 2011

Without internal affiliation

  • Author: Neuman, Benjamin W.

    University of Reading

  • Author: Kiss, Gabriella

    University of Reading

  • Author: Kunding, Andreas Hjarne

    Unknown

  • Author: Bhella, David

    Medical Research Council Virology Unit

  • Author: Baksh, M. Fazil

    University of Reading

  • Author: Connelly, Stephen

    The Scripps Research Institute

  • Author: Droese, Ben

    The Scripps Research Institute

  • Author: Klaus, Joseph P.

    University of Reading

  • Author: Makino, Shinji

    University of Texas

  • Author: Sawicki, Stanley G.

    University of Toledo

  • Author: Siddell, Stuart G.

    University of Bristol

  • Author: Stamou, Dimitrios G.

    University of Copenhagen

  • Author: Wilson, Ian A.

    The Scripps Research Institute

  • Author: Kuhn, Peter

    The Scripps Research Institute

  • Author: Buchmeier, Michael J.

    University of California

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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.
Keyword: Cryo-electron microscopy,Viral matrix protein,Coronavirus,Pleomorphic virus structure,Cryo-electron tomography
Original languageEnglish
JournalJournal of Structural Biology
Publication date2011
Volume174
Pages11-22
ISSN1047-8477
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 6
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