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Publication Abstract from PubMed

Barmah Forest virus (BFV) is a mosquito-borne alphavirus that infects humans. A 6-A-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 alpha-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.

The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions.,Kostyuchenko VA, Jakana J, Liu X, Haddow AD, Aung M, Weaver SC, Chiu W, Lok SM J Virol. 2011 Sep;85(18):9327-33. Epub 2011 Jul 13. PMID:21752915^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.