title: The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions.
abstract: 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.
authors.affiliation: Program in Emerging Infectious Diseases, Duke-NUS Graduate Medical School, 8 College Rd., 169857, Singapore.
authors.forename: Victor A
authors.initials: VA
authors.lastname: Kostyuchenko
authors.forename: Joanita
authors.initials: J
authors.lastname: Jakana
authors.forename: Xiangan
authors.initials: X
authors.lastname: Liu
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Haddow
authors.forename: Myint
authors.initials: M
authors.lastname: Aung
authors.forename: Scott C
authors.initials: SC
authors.lastname: Weaver
authors.forename: Wah
authors.initials: W
authors.lastname: Chiu
authors.forename: Shee-Mei
authors.initials: SM
authors.lastname: Lok
mesh_terms: D000524:Alphavirus / Q000648:ultrastructure*; D000818:Animals; D020285:Cryoelectron Microscopy; D006801:Humans; D021621:Imaging, Three-Dimensional; D046911:Macromolecular Substances / Q000648:ultrastructure*; D008958:Models, Molecular; D019251:Nucleocapsid / Q000648:ultrastructure; D014764:Viral Proteins / Q000648:ultrastructure*; D014771:Virion / Q000648:ultrastructure*
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins