U.S. Department of Energy Office of Biological and Environmental Research

BER Research Highlights

New Understanding of the Toxic Effects of Botulism Toxin
Published: December 20, 2004
Posted: January 03, 2005

The physical structure of a complex of the protease part of botulism toxin (botulinum neurotoxin A protease (BoNT/A)) bound to a protein (SNAP-25) has been determined, providing information about how the toxin causes paralysis. SNAP-25 is part of a protein complex that enables release of neurotransmitters that carry signals between successive cells in a nerve. BoNT/A leads to the breakdown of SNAP-25 reducing the ability of cells to release neurotransmitters resulting in paralysis. X-ray diffraction studies of crystals of the complex identified the precise interactions of BoNT/A as it interfaces with SNAP-25. This new information may lead to design of molecules that could inhibit the adverse effects of the botulism neurotoxin. Structures were determined at the Stanford Synchrotron Radiation Laboratory and the Advanced Light Source at the Lawrence Berkeley National Laboratory. The results are described in a paper published in Nature on December 16 (Nature 432, 925-929, 2004) by Stanford University scientists Mark A. Breidenbach and Axel Brunger.

Contact: Roland F. Hirsch, SC-73, (301) 903-9009
Topic Areas:

  • Research Area: Structural Biology, Biomolecular Characterization and Imaging
  • Research Area: Structural Biology Infrastructure
  • Research Area: Research Technologies and Methodologies
  • Legacy: Medical Applications

Division: SC-23.2 Biological Systems Science Division, BER
      (formerly SC-73 Medical Sciences Division, OBER)


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