Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. |
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| Authors: | I Ferlenghi M Clarke T Ruttan S L Allison J Schalich F X Heinz S C Harrison F A Rey S D Fuller |
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| Institution: | The Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. |
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| Abstract: | 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. |
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