Cellular and Molecular Life Sciences

, Volume 65, Issue 15, pp 2296–2306 | Cite as

Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins

  • A. T. BrungerEmail author
  • R. Jin
  • M. A. Breidenbach


Despite its extreme toxicity, botulinum neurotoxin is widely utilized in low doses as a treatment for several neurological disorders; higher doses cause the neuroparalytic syndrome botulism. The toxin blocks neurotransmitter release by preferentially attaching to pre-synaptic membrane receptors at neuromuscular junctions and subsequently delivering a Zn 2+-dependent protease component to presynaptic neuronal cytosol. These highly specialized enzymes exclusively hydrolyze peptide bonds within SNARE (soluble N-ethylmaleiamide sensitive factor attachment protein receptor) proteins. In this review we discuss the structural basis for botulinum toxin’s exquisite specificity for its neuronal cell-surface receptors and intracellular SNARE targets.


SNARE botulism tetanus synaptotagmin metalloprotease endocytosis synaptic vesicle neurotransmission 


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Copyright information

© Birkhaueser 2008

Authors and Affiliations

  1. 1.Howard Hughes Medical Institute and Departments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Structural Biology, and Photon ScienceStanford UniversityStanfordUSA
  2. 2.Center for Neuroscience, Aging and Stem Cell Research, Burnham institute for Medical ResearchLa JollaUSA
  3. 3.Department of ChemistryUniversity of California at BerkeleyBerkeleyUSA

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