IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-32223-1.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-32223-1
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-32223-1?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    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. 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.
    4. 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.
    Full references (including those not matched with items on IDEAS)

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    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. 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.
    3. 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.

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Zhiqiang Li & Han Xia & Guibo Rao & Yan Fu & Tingting Chong & Kexing Tian & Zhiming Yuan & Sheng Cao, 2024. "Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. 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.
    3. Liya Hu & Wilhelm Salmen & Rong Chen & Yi Zhou & Frederick Neill & James E. Crowe & Robert L. Atmar & Mary K. Estes & B. V. Venkataram Prasad, 2022. "Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32223-1. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.