Structural basis of cell surface receptor recognition by botulinum neurotoxin B

Qing Chai, Joseph W. Arndt, Min Dong, William H. Tepp, Eric A. Johnson, Edwin R. Chapman () and Raymond C. Stevens ()
Additional contact information
Qing Chai: The Scripps Research Institute
Joseph W. Arndt: The Scripps Research Institute
Min Dong: Howard Hughes Medical Institute and Department of Physiology
William H. Tepp: The University of Wisconsin
Eric A. Johnson: The University of Wisconsin
Edwin R. Chapman: Howard Hughes Medical Institute and Department of Physiology
Raymond C. Stevens: The Scripps Research Institute

Nature, 2006, vol. 444, issue 7122, 1096-1100

Abstract: Botulism toxin Botulinum toxins, produced by Clostridia botulinum, are a potential biological hazard to humans and a potential bioweapons threat. The toxins are potent inhibitors of neurotransmitter release at synapses, and it is this property that causes the neuroparalytic syndrome known as botulism. Two related papers now report the crystal structure of botulinum toxin B bound to its receptor on the exposed surface of the neuron. This will provide insight into the high affinity and specificity of this interaction, and aid in the development of antibotulism vaccines and drugs.

Date: 2006
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DOI: 10.1038/nature05411

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