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Visualizing molecular interactions that determine assembly of a bullet-shaped vesicular stomatitis virus particle

Author

Listed:
  • Simon Jenni

    (Harvard Medical School)

  • Joshua A. Horwitz

    (Harvard Medical School
    Harvard Medical School
    Molecular Pharmacology and Virology Group, PureTech Health LLC)

  • Louis-Marie Bloyet

    (Harvard Medical School
    Washington University in St. Louis)

  • Sean P. J. Whelan

    (Harvard Medical School
    Washington University in St. Louis)

  • Stephen C. Harrison

    (Harvard Medical School
    Howard Hughes Medical Institute, Harvard Medical School
    Boston Children’s Hospital)

Abstract

Vesicular stomatitis virus (VSV) is a negative-strand RNA virus with a non-segmented genome, closely related to rabies virus. Both have characteristic bullet-like shapes. We report the structure of intact, infectious VSV particles determined by cryogenic electron microscopy. By compensating for polymorphism among viral particles with computational classification, we obtained a reconstruction of the shaft (“trunk”) at 3.5 Å resolution, with lower resolution for the rounded tip. The ribonucleoprotein (RNP), genomic RNA complexed with nucleoprotein (N), curls into a dome-like structure with about eight gradually expanding turns before transitioning into the regular helical trunk. Two layers of matrix (M) protein link the RNP with the membrane. Radial inter-layer subunit contacts are fixed within single RNA-N-M1-M2 modules, but flexible lateral and axial interactions allow assembly of polymorphic virions. Together with published structures of recombinant N in various states, our results suggest a mechanism for membrane-coupled self-assembly of VSV and its relatives.

Suggested Citation

  • Simon Jenni & Joshua A. Horwitz & Louis-Marie Bloyet & Sean P. J. Whelan & Stephen C. Harrison, 2022. "Visualizing molecular interactions that determine assembly of a bullet-shaped vesicular stomatitis virus particle," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32223-1
    DOI: 10.1038/s41467-022-32223-1
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    References listed on IDEAS

    as
    1. Muchen Pan & Ana L. Alvarez-Cabrera & Joon S. Kang & Lihua Wang & Chunhai Fan & Z. Hong Zhou, 2021. "Asymmetric reconstruction of mammalian reovirus reveals interactions among RNA, transcriptional factor µ2 and capsid proteins," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    2. Ke Ding & Cristina C. Celma & Xing Zhang & Thomas Chang & Wesley Shen & Ivo Atanasov & Polly Roy & Z. Hong Zhou, 2019. "In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    3. Ambroise Desfosses & Euripedes A. Ribeiro & Guy Schoehn & Danielle Blondel & Delphine Guilligay & Marc Jamin & Rob W. H. Ruigrok & Irina Gutsche, 2013. "Self-organization of the vesicular stomatitis virus nucleocapsid into a bullet shape," Nature Communications, Nature, vol. 4(1), pages 1-5, June.
    4. Tobias Herrmann & Raúl Torres & Eric N. Salgado & Cristina Berciu & Daniel Stoddard & Daniela Nicastro & Simon Jenni & Stephen C. Harrison, 2021. "Functional refolding of the penetration protein on a non-enveloped virus," Nature, Nature, vol. 590(7847), pages 666-670, February.
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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.
    3. Friederike M. C. Benning & Simon Jenni & Coby Y. Garcia & Tran H. Nguyen & Xuewu Zhang & Luke H. Chao, 2024. "Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    4. Jack D. Whitehead & Hortense Decool & Cédric Leyrat & Loic Carrique & Jenna Fix & Jean-François Eléouët & Marie Galloux & Max Renner, 2023. "Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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