Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus.
The tick-borne encephalitis (TBE) flavivirus contains two transmembrane proteins, E and M. Coexpression of E and the M precursor (prM) leads to secretion of recombinant subviral particles (RSPs). In the most common form of these RSPs, analyzed at a 19 A resolution by cryo-electron microscopy (cryo-EM), 60 copies of E pack as dimers in a T = 1 icosahedral surface lattice (outer diameter, 315 A). Fitting the high-resolution structure of a soluble E fragment into the RSP density defines interaction sites between E dimers, positions M relative to E, and allows assignment of transmembrane regions of E and M. Lateral interactions among the glycoproteins stabilize this capsidless particle; similar interactions probably contribute to assembly of virions. The structure suggests a picture for trimer association under fusion-inducing conditions.
Ferlenghi
I
I
The Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
Clarke
M
M
Ruttan
T
T
Allison
S L
SL
Schalich
J
J
Heinz
F X
FX
Harrison
S C
SC
Rey
F A
FA
Fuller
S D
SD
D020285:Cryoelectron Microscopy; D004274:DNA, Recombinant / Q000235:genetics; D019281:Dimerization; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly
D004274:DNA, Recombinant; D011994:Recombinant Proteins; D014759:Viral Envelope Proteins; C074932:prM protein, Flavivirus; C065696:glycoprotein E, Flavivirus