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Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity

Author

Listed:
  • Rongsheng Jin

    (Howard Hughes Medical Institute
    Stanford University)

  • Andreas Rummel

    (Institut für Toxikologie)

  • Thomas Binz

    (Institut für Biochemie, Medizinische Hochschule Hannover)

  • Axel T. Brunger

    (Howard Hughes Medical Institute
    Stanford University)

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

  • Rongsheng Jin & Andreas Rummel & Thomas Binz & Axel T. Brunger, 2006. "Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity," Nature, Nature, vol. 444(7122), pages 1092-1095, December.
    • Handle: RePEc:nat:nature:v:444:y:2006:i:7122:d:10.1038_nature05387
    DOI: 10.1038/nature05387
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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.
    2. Atsushi Yamagata & Kaori Ito & Takehiro Suzuki & Naoshi Dohmae & Tohru Terada & Mikako Shirouzu, 2024. "Structural basis for antiepileptic drugs and botulinum neurotoxin recognition of SV2A," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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