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The native structure of the assembled matrix protein 1 of influenza A virus

Author

Listed:
  • Julia Peukes

    (Medical Research Council Laboratory of Molecular Biology
    European Molecular Biology Laboratory
    Heidelberg University)

  • Xiaoli Xiong

    (Medical Research Council Laboratory of Molecular Biology
    Chinese Academy of Sciences)

  • Simon Erlendsson

    (Medical Research Council Laboratory of Molecular Biology)

  • Kun Qu

    (Medical Research Council Laboratory of Molecular Biology)

  • William Wan

    (European Molecular Biology Laboratory
    Vanderbilt University)

  • Leslie J. Calder

    (The Francis Crick Institute)

  • Oliver Schraidt

    (European Molecular Biology Laboratory
    International Iberian Nanotechnology Laboratory)

  • Susann Kummer

    (Universitätsklinikum Heidelberg
    Robert Koch Institute)

  • Stefan M. V. Freund

    (Medical Research Council Laboratory of Molecular Biology)

  • Hans-Georg Kräusslich

    (Universitätsklinikum Heidelberg
    German Center for Infection Research)

  • John A. G. Briggs

    (Medical Research Council Laboratory of Molecular Biology
    European Molecular Biology Laboratory)

Abstract

Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane1. The structure of full-length M1, and how it oligomerizes to mediate the assembly of virions, is unknown. Here we determine the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We find that the C-terminal domain of M1 is disordered in solution but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerizing M1 into linear strands that coat the interior surface of the membrane of the assembling virion. In the M1 polymer, five histidine residues—contributed by three different monomers of M1—form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore reveal mechanisms of influenza virus assembly and disassembly.

Suggested Citation

  • Julia Peukes & Xiaoli Xiong & Simon Erlendsson & Kun Qu & William Wan & Leslie J. Calder & Oliver Schraidt & Susann Kummer & Stefan M. V. Freund & Hans-Georg Kräusslich & John A. G. Briggs, 2020. "The native structure of the assembled matrix protein 1 of influenza A virus," Nature, Nature, vol. 587(7834), pages 495-498, November.
    • Handle: RePEc:nat:nature:v:587:y:2020:i:7834:d:10.1038_s41586-020-2696-8
    DOI: 10.1038/s41586-020-2696-8
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    Cited by:

    1. Kang Zhou & Zhu Si & Peng Ge & Jun Tsao & Ming Luo & Z. Hong Zhou, 2022. "Atomic model of vesicular stomatitis virus and mechanism of assembly," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Lu Xue & Tiancai Chang & Zimu Li & Chenchen Wang & Heyu Zhao & Mei Li & Peng Tang & Xin Wen & Mengmeng Yu & Jiqin Wu & Xichen Bao & Xiaojun Wang & Peng Gong & Jun He & Xinwen Chen & Xiaoli Xiong, 2024. "Cryo-EM structures of Thogoto virus polymerase reveal unique RNA transcription and replication mechanisms among orthomyxoviruses," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    3. Bryan S. Sibert & Joseph Y. Kim & Jie E. Yang & Zunlong Ke & Christopher C. Stobart & Martin L. Moore & Elizabeth R. Wright, 2024. "Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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