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The 3D structure of the fusion primed Sendai F-protein determined by electron cryomicroscopy

Kai Ludwig1, Bolormaa Baljinnyam, Andreas Herrmann

  • 1Forschungszentrum für Elektronenmikroskopie, Freie Universität Berlin, Berlin, Germany.

The EMBO Journal
|July 26, 2003
PubMed

Insights

Researchers determined the 3D structure of Sendai virus fusion F protein using cryo-electron microscopy. The structure reveals a conformation suggesting an advanced state towards fusion activity.

Area of Science:

  • Structural biology
  • Virology
  • Molecular biology

Background:

  • The fusion (F) protein of paramyxoviruses mediates viral entry into host cells.
  • Understanding the F protein structure is crucial for developing antiviral strategies.

Purpose of the Study:

  • To determine the three-dimensional (3D) structure of the Sendai virus fusion F protein ectodomain.
  • To elucidate the structural basis of F protein-mediated membrane fusion.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of single molecules.
  • Three-dimensional (3D) reconstruction at approximately 16 Å resolution.
  • Analysis of the native, proteolytically processed F1+F2 form.

Main Results:

  • The 3D structure of the Sendai virus F protein ectodomain (homotrimeric, ~177 kDa) was determined.
  • The structure shows the protein protruding ~170 Å from the membrane, featuring a head, neck, and stalk.
  • Structural comparison with Newcastle disease virus F protein suggests an advanced fusion-active conformation.

Conclusions:

  • The determined structure provides insights into the Sendai virus F protein's conformation.
  • Structural differences compared to other paramyxovirus F proteins highlight unique features.
  • This structure represents a potential intermediate state leading to membrane fusion.

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