Skip to main content
Log in

Direct evidence for the specific fixation of Cl. Botulinum A neurotoxin to brain matter

  • Published:
Naunyn-Schmiedeberg's Archives of Pharmacology Aims and scope Submit manuscript

Summary

  1. 1.

    Rat brain homogenate and synaptosomes from rat brain bind botulinum toxin. The binding is accompanied by partial inactivation. The binding decreases with increasing ionic strength. A considerable fixation of tetanus toxin can still be demonstrated under conditions which prevent the fixation of botulinum toxin.

  2. 2.

    Only the grey substance, not the white substance from bovine brain is able to bind the toxin.

  3. 3.

    Upon pretreatment with neuraminidase, synaptosomes lose nearly all of their binding capacity. However, neither gangliosides nor ganglioside-cerebroside mixtures nor brain extracts could replace the synaptosomes.

Thus botulinum A toxin closely resembles tetanus toxin in its ability to react with (a) neuraminidase-sensitive site(s) of the grey matter of the CNS. It differs from tetanus toxin by its stronger sensitivity against ionic forces and by its failure to react with certain gangliosides.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Boroff, D. A., Fleck, U.: Statistical analysis of a rapidin vivo method for the titration of the toxin of clostridium botulinum. J. Bact.92, 1580–1581 (1966)

    Google Scholar 

  • Brownlee, K. A.: Statistical theory and methodology. New York: Wiley 1965

    Google Scholar 

  • Habermann, E.: Interaction of labelled tetanus toxin and toxoid with substructures of rat brain and psinal cordin vitro. Naunyn-Schmiedeberg's Arch. Pharmacol.276, 341–359 (1973)

    Google Scholar 

  • Habermann, E.:125I-labeled neurotoxin from clostridium botulinum A: Preparation, binding to synaptosomes and ascent to the spinal cord. Naunyn-Schmiedeberg's Arch. Pharmacol.281, 47–56 (1974)

    Google Scholar 

  • Mellanby, J., Thompson, P. A., Hampden, N.: On the similarity of tetanus and botulinum toxins. Naunyn-Schmiedeberg's Arch. Pharmacol.276, 303–310 (1973)

    Google Scholar 

  • Simpson, L. L., Rapport, M. M.: Ganglioside inactivation of botulinum toxin. J. Neurochem.18, 1341–1343 (1971a)

    Google Scholar 

  • Simpson, L. L., Rapport, M. M.: The binding of botulinum toxin to membrane lipids: Sphingolipids, steroids and fatty acids. J. Neurochem.17, 1751–1759 (1971b)

    Google Scholar 

  • Simpson, L. L., Rapport, M. M.: The binding of botulinum toxin to membrane lipids: Phospholipids and proteolipid. J. Neurochem.18, 1761–1767 (1971c)

    Google Scholar 

  • van Heyningen, W. E., Mellanby, J.: The effect of cerebroside and other lipids on the fixation of tetanus toxin by gangliosides. J. gen. Microbiol.52, 447–454 (1968)

    Google Scholar 

  • van Heyningen, W. E., Mellanby, J.: A note on the specific fixation, specific deactivation and non-specific inactivation of bacterial toxins by gangliosides. Naunyn-Schmiedeberg's Arch. Pharmacol.276, 297–302 (1973)

    Google Scholar 

  • Whittaker, V. P.: The synaptosomes. In: A. Lajtha (ed.): Handbook of Neurochemistry, Vol. II, pp. 327–364. New York-London: Plenum Press 1969

    Google Scholar 

  • Wiegand, H., Wellhöner, H. H.: Type A botulinum toxin in cats: Neural ascent and action on spinal cord reflexes. Naunyn-Schmiedeberg's Arch. Pharmacol.282, R 106 (1974)

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Habermann, E., Heller, I. Direct evidence for the specific fixation of Cl. Botulinum A neurotoxin to brain matter. Naunyn-Schmiedeberg's Arch. Pharmacol. 287, 97–106 (1975). https://doi.org/10.1007/BF00632641

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00632641

Key words

Navigation