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Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A

Author

Listed:
  • Roger M. Benoit

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Daniel Frey

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Manuel Hilbert

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Josta T. Kevenaar

    (Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands)

  • Mara M. Wieser

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Christian U. Stirnimann

    (Swiss Light Source, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • David McMillan

    (UCB Celltech, UCB Pharma, UCB NewMedicines, Slough SL1 4EN, UK)

  • Tom Ceska

    (UCB Celltech, UCB Pharma, UCB NewMedicines, Slough SL1 4EN, UK)

  • Florence Lebon

    (UCB Pharma, UCB NewMedicines, B-1420 Braine-L’Alleud, Belgium)

  • Rolf Jaussi

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Michel O. Steinmetz

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Gebhard F. X. Schertler

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
    ETH Zurich, CH-8093 Zurich, Switzerland)

  • Casper C. Hoogenraad

    (Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands)

  • Guido Capitani

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

  • Richard A. Kammerer

    (Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland)

Abstract

Botulinum neurotoxin A (BoNT/A) is considered the most toxic substance known but is also used as a therapeutic drug for a growing number of diseases and conditions; researchers have now obtained a high-resolution crystal structure of the receptor-binding domain of the BoNT/A in complex with the luminal domain of synaptic vesicle protein 2C (SV2C), one of its receptors, allowing the identification of a peptide that can inhibit complex formation.

Suggested Citation

  • Roger M. Benoit & Daniel Frey & Manuel Hilbert & Josta T. Kevenaar & Mara M. Wieser & Christian U. Stirnimann & David McMillan & Tom Ceska & Florence Lebon & Rolf Jaussi & Michel O. Steinmetz & Gebhar, 2014. "Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A," Nature, Nature, vol. 505(7481), pages 108-111, January.
    • Handle: RePEc:nat:nature:v:505:y:2014:i:7481:d:10.1038_nature12732
    DOI: 10.1038/nature12732
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    Citations

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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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