The Fusion Glycoprotein Shell of Semliki Forest Virus An Icosahedral Assembly Primed for Fusogenic Activation at Endosomal pH

@article{Lescar2001TheFG,
  title={The Fusion Glycoprotein Shell of Semliki Forest Virus An Icosahedral Assembly Primed for Fusogenic Activation at Endosomal pH},
  author={Julien Lescar and Alain Roussel and Michelle W. Wien and Jorge Navaza and Stephen D. Fuller and Gisela Wengler and Gerd Wengler and F{\'e}lix A Rey},
  journal={Cell},
  year={2001},
  volume={105},
  pages={137-148}
}
Semliki Forest virus (SFV) has been extensively studied as a model for analyzing entry of enveloped viruses into target cells. Here we describe the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its interactions at the surface of the virus. E1 is unexpectedly similar to the flavivirus envelope protein, with three structural domains disposed in the same primary sequence arrangement. These results introduce… CONTINUE READING

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