Changing the Receptor Specificity of Anthrax Toxin

@inproceedings{Mechaly2012ChangingTR,
  title={Changing the Receptor Specificity of Anthrax Toxin},
  author={Adva Mechaly and Andrew J. McCluskey and Robert J. Collier},
  booktitle={mBio},
  year={2012}
}
UNLABELLED The actions of many bacterial toxins depend on their ability to bind to one or more cell-surface receptors. Anthrax toxin acts by a sequence of events that begins when the protective-antigen (PA) moiety of the toxin binds to either one of two cell-surface proteins, ANTXR1 and ANTXR2, and is proteolytically activated. The activated PA self-associates to form oligomeric pore precursors, which, in turn, bind the enzymatic moieties of the toxin and transport them to the cytosol. We… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 18 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 37 references

Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles

  • H Katayama
  • Proc. Natl. Acad. Sci
  • 2010
2 Excerpts

Similar Papers

Loading similar papers…