Cryo-electron microscopy study of bacteriophage T4 displaying anthrax toxin proteins.

@article{Fokine2007CryoelectronMS,
  title={Cryo-electron microscopy study of bacteriophage T4 displaying anthrax toxin proteins.},
  author={Andrei Fokine and Valorie D. Bowman and Anthony J. Battisti and Qin Li and Paul R. Chipman and Venigalla Rao and Michael G. Rossmann},
  journal={Virology},
  year={2007},
  volume={367 2},
  pages={422-7}
}
The bacteriophage T4 capsid contains two accessory surface proteins, the small outer capsid protein (Soc, 870 copies) and the highly antigenic outer capsid protein (Hoc, 155 copies). As these are dispensable for capsid formation, they can be used for displaying proteins and macromolecular complexes on the T4 capsid surface. Anthrax toxin components were attached to the T4 capsid as a fusion protein of the N-terminal domain of the anthrax lethal factor (LFn) with Soc. The LFn-Soc fusion protein… CONTINUE READING