Structure of correctly self-assembled bluetongue virus-like particles.
Bluetongue virus-like particles (VLPs), synthesized by coexpression of VP2, VP3, VP5, and VP7 using recombinant baculoviruses, have been examined by cryoelectron microscopy and image analysis. The 3-D reconstruction of these VLPs reveals an icosahedral structure 86 nm in diameter with essentially the same features as for the native Bluetongue virus (BTV) particle. The VLP is thus shown to contain the four constituent proteins as the native virus particle, with each of the protein positions highly occupied. Since the BTV core-like particle formed by coexpression of VP3 and VP7 lacks five VP7 trimers around each of the five-fold axes, it appears that the presence of the outer capsid proteins VP2 and VP5 is necessary for the adhesion of these VP7 trimers around the five-fold axes. The observed spontaneous formation of complete VLP in the absence of the BTV nonstructural proteins implies that the nonstructural proteins are not necessary for the formation of the double-shelled viral capsid. However, the nonstructural proteins may be involved in different aspects of genome replication and packaging.
Hewat
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EA
Institut de Biologie Structurale, Grenoble, France.
Booth
T F
TF
Roy
P
P
D016367:Baculoviridae; D001820:Bluetongue virus / Q000254:growth & development / Q000648:ultrastructure*; D005583:Fourier Analysis; D008854:Microscopy, Electron / Q000379:methods; D008961:Models, Structural; D012330:RNA, Double-Stranded / Q000648:ultrastructure; D014758:Viral Core Proteins / Q000096:biosynthesis / Q000648:ultrastructure
D012330:RNA, Double-Stranded; D014758:Viral Core Proteins