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Promotion of virus assembly and organization by the measles virus matrix protein

Author

Listed:
  • Zunlong Ke

    (Children’s Healthcare of Atlanta
    Georgia Institute of Technology)

  • Joshua D. Strauss

    (Children’s Healthcare of Atlanta)

  • Cheri M. Hampton

    (Children’s Healthcare of Atlanta)

  • Melinda A. Brindley

    (University of Georgia
    Georgia State University)

  • Rebecca S. Dillard

    (Children’s Healthcare of Atlanta)

  • Fredrick Leon

    (Children’s Healthcare of Atlanta)

  • Kristen M. Lamb

    (Children’s Healthcare of Atlanta)

  • Richard K. Plemper

    (Georgia State University)

  • Elizabeth R. Wright

    (Children’s Healthcare of Atlanta
    Robert P. Apkarian Integrated Electron Microscopy Core, Emory University)

Abstract

Measles virus (MeV) remains a major human pathogen, but there are presently no licensed antivirals to treat MeV or other paramyxoviruses. Here, we use cryo-electron tomography (cryo-ET) to elucidate the principles governing paramyxovirus assembly in MeV-infected human cells. The three-dimensional (3D) arrangement of the MeV structural proteins including the surface glycoproteins (F and H), matrix protein (M), and the ribonucleoprotein complex (RNP) are characterized at stages of virus assembly and budding, and in released virus particles. The M protein is observed as an organized two-dimensional (2D) paracrystalline array associated with the membrane. A two-layered F–M lattice is revealed suggesting that interactions between F and M may coordinate processes essential for MeV assembly. The RNP complex remains associated with and in close proximity to the M lattice. In this model, the M lattice facilitates the well-ordered incorporation and concentration of the surface glycoproteins and the RNP at sites of virus assembly.

Suggested Citation

  • Zunlong Ke & Joshua D. Strauss & Cheri M. Hampton & Melinda A. Brindley & Rebecca S. Dillard & Fredrick Leon & Kristen M. Lamb & Richard K. Plemper & Elizabeth R. Wright, 2018. "Promotion of virus assembly and organization by the measles virus matrix protein," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04058-2
    DOI: 10.1038/s41467-018-04058-2
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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. 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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