High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains

Umesh Katpally, Neil R. Voss, Tommaso Cavazza, Stefan Taube, John R. Rubin, Vivienne L. Young, Jeanne Stuckey, Vernon K. Ward, Herbert W. Virgin IV, Christiane E. Wobus, Thomas J. Smith

Research output: Contribution to journalArticle

47 Scopus citations

Abstract

Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the threedimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to ∼8-Å resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.

Original languageEnglish (US)
Pages (from-to)5836-5841
Number of pages6
JournalJournal of virology
Volume84
Issue number11
DOIs
StatePublished - Jun 2010
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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    Katpally, U., Voss, N. R., Cavazza, T., Taube, S., Rubin, J. R., Young, V. L., Stuckey, J., Ward, V. K., Virgin IV, H. W., Wobus, C. E., & Smith, T. J. (2010). High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. Journal of virology, 84(11), 5836-5841. https://doi.org/10.1128/JVI.00314-10