Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry

@inproceedings{Fabre2016StructureOA,
  title={Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry},
  author={Lucien Fabre and Eugenio Santelli and Driss Mountassif and Annemarie Donoghue and Aviroop Biswas and Rikard Blunck and Dorit Hanein and Niels Volkmann and Robert C. Liddington and Isabelle Rouiller},
  booktitle={The Journal of general physiology},
  year={2016}
}
Anthrax toxin comprises three soluble proteins: protective antigen (PA), lethal factor (LF), and edema factor (EF). PA must be cleaved by host proteases before it oligomerizes and forms a prepore, to which LF and EF bind. After endocytosis of this tripartite complex, the prepore transforms into a narrow transmembrane pore that delivers unfolded LF and EF into the host cytosol. Here, we find that translocation of multiple 90-kD LF molecules is rapid and efficient. To probe the molecular basis of… CONTINUE READING

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