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Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins

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Abstract.

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.

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Author notes

  1. R. Jin

    Present address: Center for Neuroscience, Aging and Stem Cell Research, Burnham institute for Medical Research, La Jolla, CA, 92037, USA

  2. M. A. Breidenbach

    Present address: Department of Chemistry, University of California at Berkeley, Berkeley, CA, 94720, USA

Authors and Affiliations

  1. Howard Hughes Medical Institute and Departments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Structural Biology, and Photon Science, Stanford University, Stanford, CA, 94305, USA

    A. T. Brunger, R. Jin & M. A. Breidenbach

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  1. A. T. Brunger
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  2. R. Jin
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  3. M. A. Breidenbach
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Corresponding author

Correspondence to A. T. Brunger.

Additional information

Received 20 February 2008; received after revision 4 March 2008; accepted 6 March 2008

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Brunger, A.T., Jin, R. & Breidenbach, M.A. Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins. Cell. Mol. Life Sci. 65, 2296–2306 (2008). https://doi.org/10.1007/s00018-008-8088-0

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  • DOI: https://doi.org/10.1007/s00018-008-8088-0

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