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Structural basis of cell surface receptor recognition by botulinum neurotoxin B

Author

Listed:
  • 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)

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.

Suggested Citation

  • Qing Chai & Joseph W. Arndt & Min Dong & William H. Tepp & Eric A. Johnson & Edwin R. Chapman & Raymond C. Stevens, 2006. "Structural basis of cell surface receptor recognition by botulinum neurotoxin B," Nature, Nature, vol. 444(7122), pages 1096-1100, December.
    • Handle: RePEc:nat:nature:v:444:y:2006:i:7122:d:10.1038_nature05411
    DOI: 10.1038/nature05411
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    Cited by:

    1. Zheng Liu & Pyung-Gang Lee & Nadja Krez & Kwok-ho Lam & Hao Liu & Adina Przykopanski & Peng Chen & Guorui Yao & Sicai Zhang & Jacqueline M. Tremblay & Kay Perry & Charles B. Shoemaker & Andreas Rummel, 2023. "Structural basis for botulinum neurotoxin E recognition of synaptic vesicle protein 2," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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