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Neurotransmission

Wrinklefree and deadly: BoNTs

Nature Reviews Neuroscience volume 8, page 88 (2007)Cite this article

Regardless of whether botulinum neurotoxins (BoNTs) are accidentally ingested with disastrous consequences or whether vanity drives people to inject them to smooth their wrinkles, the molecular mechanism by which these toxins bind to neurons has remained elusive. Three new papers now present structural and mutational analyses of the molecular interactions of BoNT/B and G, with synaptotagmins and gangliosides as the two distinct receptors on the neuronal membrane, confirming the long-standing double-receptor hypothesis.

There are seven structurally and functionally related serotypes of bacterial BoNTs (BoNT/A–G), which bind to motor neurons with very high affinity. After undergoing receptor-mediated endocytosis, they translocate from the endosome to the cytosol. There they proteolytically cleave core proteins of the vesicle fusion machinery, leading to inhibition of neurotransmission at the neuromuscular junction, causing muscle paralysis.

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ORIGINAL RESEARCH PAPERS

  1. Rummel, A. et al. Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept. PNAS 104, 359–364 (2007)

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  2. Jin, R. et al. Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444, 1092–1095 (2006)

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  3. Chai, Q. et al. Structural basis of cell surface receptor recognition by botulinum neurotoxin B. Nature 444, 1096–1100 (2006)

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  4. Garcia-Rodriguez, C. et al. Molecular evolution of antibody cross-reactivity for two subtypes of type A botulinum neurotoxin. Nature Biotech. 25, 107–116 (2007)

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Authors
  1. Claudia Wiedemann
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Wiedemann, C. Wrinklefree and deadly: BoNTs. Nat Rev Neurosci 8, 88 (2007). https://doi.org/10.1038/nrn2085

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