title: Structure of bluetongue virus particles by cryoelectron microscopy.
abstract: The structure of the bluetongue virus (BTV) particle, determined by cryoelectron microscopy and image analysis, reveals a well-ordered outer shell which differs markedly from other known Reoviridae. The inner shell is known to have an icosahedral structure with 260 triangular spikes of VP7 trimers arranged on a T = 13,l lattice. The outer shell is seen to consist of 120 globular regions (possibly VP5), which sit neatly on each of the six-membered rings of VP7 trimers. "Sail"-shaped spikes located above 180 of the VP7 trimers form 60 triskelion-type motifs which cover all but 20 of the VP7 trimers. These spikes are possibly the hemagglutinating protein VP2 which contains a virus neutralization epitope. Thus, VP2 and VP5 together form a continuous layer around the inner shell except for holes on the 5-fold axis.
authors.affiliation: Laboratoire de Biologie Structurale, CEA and CNRS URA 1333, Grenoble, France.
authors.forename: E A
authors.initials: EA
authors.lastname: Hewat
authors.forename: T F
authors.initials: TF
authors.lastname: Booth
authors.forename: P
authors.initials: P
authors.lastname: Roy
mesh_terms: D001820:Bluetongue virus / Q000648:ultrastructure*; D002213:Capsid / Q000648:ultrastructure; D005615:Freezing; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron / Q000379:methods; D015678:Viral Structural Proteins / Q000648:ultrastructure; D014771:Virion / Q000648:ultrastructure
chemical_list: D015678:Viral Structural Proteins