Partial Characterization of Bovine Synaptosomal Proteins Adhered to By Botulinum and Tetanus Neurotoxins
Binding of botulinum (BTx) and tetanus (TTx) neurotoxins to synaptic termini has been hypothesized to require a protein component(s)1–3 in addition to gangliosides of the Glb series4,5 (nomenclature described by Svennerhoim6). Results that we obtained in studies of inhibition by gangliosides of the binding of BTxA and TTx to ganglioside GT1b-coated plastic wells indicate that Glb gangliosides do not function as high affinity ligands for the neurotoxins. We observed that the concentration of ganglioside GT1b needed to block binding of either BTxA or TTx to GT1bcoated plastic wells was in the µM range.7 In contrast, when the same assay system was used to determine the concentration of ganglioside GM1 needed to block binding of cholera toxin to GM1-coated plastic wells, nM values were obtained.8
KeywordsAmmonium Sulfate Cholera Toxin Electric Organ Tetanus Toxin High Affinity Ligand
Unable to display preview. Download preview PDF.
- 10.C. Solsona, G. Egea, J. Blasi, C. Casanova, and J. Marsal, The action of botulinum toxin on cholinergic nerve terminals isolated from the electric organ ofTorpedo marmorata. Detection of a putative toxin receptor, J. Physiol. (Paris) 84: 174 (1990).Google Scholar
- 13.C-L. Schengrund, N.J. Ringler, and B.R. DasGupta, Adherence of botulinum and tetanus neurotoxins to synaptosomal proteins, Brain Res. Bull. (in press).Google Scholar