Structure of bluetongue virus particles by cryoelectron microscopy.
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.
Hewat
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Laboratoire de Biologie Structurale, CEA and CNRS URA 1333, Grenoble, France.
Booth
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Roy
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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
D015678:Viral Structural Proteins