Evidence for direct binding of Clostridium botulinum type E derivative toxin and its fragments to gangliosides and free fatty acids

Biochem Biophys Res Commun. 1986 Nov 14;140(3):1015-9. doi: 10.1016/0006-291x(86)90736-9.

Abstract

Clostridium botulinum type E derivative toxin and its heavy chain bound to gangliosides GT1b, GD1a and GQ1b and saturated and unsaturated free fatty acids with chain lengths of 14-20 carbons. The L-H-1 fragment lacking the carboxyl-terminal portion of the heavy chain bound to free fatty acids but not to gangliosides. These observations led us to a new hypothesis on the mechanism of binding between botulinum toxin and gangliosides; the carboxyl-terminal portion (H-2 fragment) of the heavy chain binds to an oligosaccharide residue of gangliosides and then the amino-terminal portion (H-1 fragment) interacts with the hydrophobic portion of gangliosides consisting of fatty acids.

MeSH terms

  • Binding Sites
  • Botulinum Toxins / metabolism*
  • Chromatography, Thin Layer
  • Fatty Acids, Nonesterified / metabolism*
  • Gangliosides / metabolism*
  • Immunochemistry
  • Peptide Fragments / metabolism*
  • Protein Binding

Substances

  • Fatty Acids, Nonesterified
  • Gangliosides
  • Peptide Fragments
  • Botulinum Toxins