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Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus

I Ferlenghi1, M Clarke, T Ruttan

  • 1The Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.

Molecular Cell
|July 21, 2001
PubMed

Insights

The tick-borne encephalitis virus (TBEV) E and M proteins form recombinant subviral particles (RSPs). Cryo-electron microscopy reveals their icosahedral structure, aiding understanding of TBEV assembly and fusion mechanisms.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Tick-borne encephalitis virus (TBEV) is a significant human pathogen.
  • TBEV possesses two transmembrane proteins, E and M, crucial for viral structure and assembly.
  • Recombinant subviral particles (RSPs) are valuable tools for studying flavivirus structure.

Purpose of the Study:

  • To determine the high-resolution structure of TBEV RSPs.
  • To elucidate the interactions between the E and M proteins within RSPs.
  • To gain insights into the assembly and fusion mechanisms of TBEV.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) at 19 Å resolution.
  • Analysis of recombinant subviral particles (RSPs) produced by coexpressing E and prM proteins.
  • Fitting of high-resolution soluble E fragment structures into the RSP density map.

Main Results:

  • The TBEV RSP structure exhibits T = 1 icosahedral symmetry with 60 E protein dimers.
  • Detailed mapping of E-E dimer interactions and M protein positioning relative to E.
  • Identification of transmembrane regions for both E and M glycoproteins.

Conclusions:

  • Lateral glycoprotein interactions stabilize the capsidless TBEV RSPs.
  • These interactions are likely essential for the assembly of infectious TBEV virions.
  • The determined structure provides a model for E protein trimer association during fusion.

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