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Updated: Jul 26, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
The transglutaminase hypothesis for the action of tetanus toxin
F Facchiano1, F Valtorta, F Benfenati
1Laboratory of Molecular Neurobiology, Mario Negri Institute of Pharmacological Research, Consorzio Mario Negri Sud, S. Maria Imbaro (Chieti), Italy.
Abstract:
Tetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca(2+)-dependent enzyme that can form stable crosslinks between substrate proteins. Transglutaminase is present in nerve terminals and recognizes synapsin I, an abundant synaptic vesicle phosphoprotein involved in neurotransmission, as an excellent substrate. The neuroparalytic action of tetanus toxin might be due, at least in part, to the stimulation of synaptic transglutaminase and the consequent crosslinking of synapsin I.
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