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Structural biology

Dangerous liaisons on neurons

Nature volume 444, pages 1019–1020 (2006)Cite this article

Crystal structures show that botulinum toxins bind simultaneously to two sites on neurons. This dual interaction allows them to use a Trojan-horse strategy to enter nerve terminals, with deadly effect.

Botulinum neurotoxins (BoNTs) are some of the most deadly substances known to mankind. By blocking nerve function, they cause botulism, a severe condition that may ultimately lead to muscular and respiratory paralysis. These sophisticated bacterial proteins owe their toxicity to their extraordinary specificity for neurons and to their enzymatic activity. In this issue, papers by Jin et al.1 and Chai et al.2 describe the mechanisms by which BoNT/B — a toxin that causes human botulism — recognizes the surface of neuron junctions (synapses)Footnote 1. This work provides insight into how other BoNTs may exert their lethal action, and describes a mode of binding that might be used by other biological compounds.

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Figure 1: Possible binding sites of botulinum neurotoxin B (BoNT/B) on neurons.

Notes

  1. This article and the papers concerned1,2 were published online on 13 December 2006.

References

  1. Jin, R., Rummel, A., Binz, T. & Brunger, A. T. Nature 444, 1092–1095 (2006).

    Article  ADS  CAS  Google Scholar 

  2. Chai, Q. et al. Nature 444, 1096–1100 (2006).

    Article  ADS  CAS  Google Scholar 

  3. Schiavo, G., Matteoli, M. & Montecucco, C. Physiol. Rev. 80, 717–766 (2000).

    Article  CAS  Google Scholar 

  4. Montecucco, C. Trends Biochem. Sci. 11, 314–317 (1986).

    Article  CAS  Google Scholar 

  5. Nishiki, T. et al. FEBS Lett. 378, 253–257 (1996).

    Article  CAS  Google Scholar 

  6. Dong, M. et al. J. Cell Biol. 162, 1293–1303 (2003).

    Article  CAS  Google Scholar 

  7. Rummel, A., Karnath, T., Henke, T., Bigalke, H. & Binz, T. J. Biol. Chem. 279, 30865–30870 (2004).

    Article  CAS  Google Scholar 

  8. Dong, M. et al. Science 312, 592–596 (2006).

    Article  ADS  CAS  Google Scholar 

  9. Mahrhold, S., Rummel, A., Bigalke, H., Davletov, B. & Binz, T. FEBS Lett. 580, 2011–2014 (2006).

    Article  CAS  Google Scholar 

  10. Rummel, A. et al. Proc. Natl Acad. Sci. USA (in the press).

  11. Fernandez-Alfonso, T., Kwan, R. & Ryan, T. A. Neuron 51, 149–151 (2006).

    Article  Google Scholar 

  12. Deinhardt, K., Berninghausen, O., Willison, H. J., Hopkins, C. R. & Schiavo, G. J. Cell Biol. 174, 459–471 (2006).

    Article  CAS  Google Scholar 

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  1. Molecular Neuropathobiology Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK

    Giampietro Schiavo

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  1. Giampietro Schiavo
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Schiavo, G. Dangerous liaisons on neurons. Nature 444, 1019–1020 (2006). https://doi.org/10.1038/nature05410

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