The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions

J Virol. 2011 Sep;85(18):9327-33. doi: 10.1128/JVI.05015-11. Epub 2011 Jul 13.


Barmah Forest virus (BFV) is a mosquito-borne alphavirus that infects humans. A 6-Å-resolution cryo-electron microscopy three-dimensional structure of BFV exhibits a typical alphavirus organization, with RNA-containing nucleocapsid surrounded by a bilipid membrane anchored with the surface proteins E1 and E2. The map allows details of the transmembrane regions of E1 and E2 to be seen. The C-terminal end of the E2 transmembrane helix binds to the capsid protein. Following the E2 transmembrane helix, a short α-helical endodomain lies on the inner surface of the lipid envelope. The E2 endodomain interacts with E1 transmembrane helix from a neighboring E1-E2 trimeric spike, thereby acting as a spacer and a linker between spikes. In agreement with previous mutagenesis studies, the endodomain plays an important role in recruiting other E1-E2 spikes to the budding site during virus assembly. The E2 endodomain may thus serve as a target for antiviral drug design.

Publication types

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

MeSH terms

  • Alphavirus / ultrastructure*
  • Animals
  • Cryoelectron Microscopy
  • Humans
  • Imaging, Three-Dimensional
  • Macromolecular Substances / ultrastructure*
  • Models, Molecular
  • Nucleocapsid / ultrastructure
  • Viral Proteins / ultrastructure*
  • Virion / ultrastructure*


  • Macromolecular Substances
  • Viral Proteins

Associated data

  • PDB/2YEW