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TitleThe structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions.
Journal, issue, pagesJ Virol, Vol. 85, Issue 18, Page 9327-9333, Year 2011
Publish dateJul 13, 2011
AuthorsVictor A Kostyuchenko / Joanita Jakana / Xiangan Liu / Andrew D Haddow / Myint Aung / Scott C Weaver / Wah Chiu / Shee-Mei Lok /
PubMed AbstractBarmah 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, ...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.
External linksJ Virol / PubMed:21752915 / PubMed Central
MethodsEM (single particle)
Resolution5 - 6.0 Å
Structure data

1886

2yew

EMDB-1886: The 6A cryo-EM reconstruction of Barmah Forest virus
PDB-2yew: Modeling Barmah Forest virus structural proteins
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • barmah forest virus
KeywordsVIRUS / ALPHAVIRUS / MOLECULAR DYNAMICS

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