IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v430y2004i7003d10.1038_nature02836.html
   My bibliography  Save this article

Structural rearrangements in the membrane penetration protein of a non-enveloped virus

Author

Listed:
  • Philip R. Dormitzer

    (Harvard Medical School, and the Laboratory of Molecular Medicine, Children's Hospital)

  • Emma B. Nason

    (Baylor College of Medicine)

  • B. V. Venkataram Prasad

    (Baylor College of Medicine)

  • Stephen C. Harrison

    (Harvard Medical School, and the Laboratory of Molecular Medicine, Children's Hospital
    Howard Hughes Medical Institute)

Abstract

Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year1. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes2. We have determined the crystal structure, at 3.2 Å resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a ∼12 Å resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses3,4,5,6.

Suggested Citation

  • Philip R. Dormitzer & Emma B. Nason & B. V. Venkataram Prasad & Stephen C. Harrison, 2004. "Structural rearrangements in the membrane penetration protein of a non-enveloped virus," Nature, Nature, vol. 430(7003), pages 1053-1058, August.
    • Handle: RePEc:nat:nature:v:430:y:2004:i:7003:d:10.1038_nature02836
    DOI: 10.1038/nature02836
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature02836
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature02836?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    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:nature:v:430:y:2004:i:7003:d:10.1038_nature02836. 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.

    We have no bibliographic references for this item. You can help adding them by using 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.