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

J Virol. 2010 Jun;84(11):5836-41. doi: 10.1128/JVI.00314-10. Epub 2010 Mar 24.


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 three-dimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to approximately 8-A 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Cryoelectron Microscopy / methods*
  • Hemorrhagic Disease Virus, Rabbit / chemistry*
  • Imaging, Three-Dimensional
  • Mice
  • Norovirus / chemistry*
  • Pliability
  • Protein Conformation
  • Rabbits
  • Receptors, Virus / chemistry*


  • Receptors, Virus