Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc.

  title={Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc.},
  author={G. Schiavo and B. Poulain and O. Rossetto and F. Benfenati and L. Tauc and C. Montecucco},
  journal={The EMBO Journal},
Tetanus and botulinum neurotoxins are the most potent toxins known. They bind to nerve cells, penetrate the cytosol and block neurotransmitter release. Comparison of their predicted amino acid sequences reveals a highly conserved segment that contains the HexxH zinc binding motif of metalloendopeptidases. The metal content of tetanus toxin was then measured and it was found that one atom of zinc is bound to the light chain of tetanus toxin. Zinc could be reversibly removed by incubation with… Expand
Tetanus and Botulinum Neurotoxins Are Zinc Proteases Specific for Components of the Neuroexocytosis Apparatus a
From these studies, it can be concluded that the clostridial neurotoxins responsible for tetanus and botulism block neuroexocytosis via the proteolytic cleavage of specific components of the neuroxocytotic machinery. Expand
Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals
The results indicate that zinc bound to the zinc binding motif constitutes the active site of the tetanus toxin light chain and suggest that cleavage of synaptobrevin by the neurotoxin causes the inhibition of exocytotic release of vasopressin from secretory granules. Expand
Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
The results indicate that tetanus and botulinum B neurotoxins block neurotransmitter release by cleaving synaptobrevin-2, a protein that, on the basis of the results, seems to play a key part in neurotransmitterRelease. Expand
Functional characterization of the catalytic site of the tetanus toxin light chain using permeabilized adrenal chromaffin cells
These data show that zinc and the putative zinc binding domain constitute the active site of the tetanus toxin light chain, and suggest that synaptobrevins are not a major target of tetanus toxins in adrenal chromaffin cells. Expand
Botulinum A Like Type B and Tetanus Toxins Fulfils Criteria for Being a Zinc‐Dependent Protease
Various criteria establish that a zinc‐dependent protease activity underlies the neurotoxicity of BoNT/A, a finding confirmed at motor nerve endings for type B and TeTx, which necessitate the design of improved inhibitors for possible use in the clinical treatment of tetanus or botulism. Expand
The metallo-proteinase activity of tetanus and botulism neurotoxins
The target specificity of these metallo-proteinases relies on a double recognition of their substrates based on interactions with the cleavage site and with a non-contiguous segment that contains a structural motif common to VAMP, SNAP-25 and syntaxin. Expand
Tetanus Toxin Inhibits Neuroexocytosis Even When Its Zn-dependent Protease Activity Is Removed (*)
It is concluded that TeTX inhibits neurotransmitter release by proteolysis of Sbr and a protease-independent activation of a neuronal TGase. Expand
Molecular aspects of tetanus and botulinum neurotoxin poisoning
Clostridial neurotoxins have now become powerful tools to investigate the final events occurring during secretion in neuronal, endocrine, and non-neuronal cells and are applied to dissect the specific interactions of the SNARE protein complex with cytosolic fusogens and other modulators of exocytosis. Expand
Metallopeptidase inhibitors of tetanus toxin: A combinatorial approach.
Combinatorial libraries of pseudotripeptides, containing an ethylene sulfonamide or an m-sulfonamidophenyl moiety as the P1 side chain and natural amino acids in P1 and P2' positions, were synthesized and the best inhibitory activity was observed with Tyr and His as P1' and P 2' components, respectively. Expand
Structure and function of tetanus and botulinum neurotoxins.
Tetanus and botulinum neurotoxins form a new group of zinc-endopeptidases with characteristic sequence, mode of zinc coordination, mechanism of activation and target recognition, of great value in the unravelling of the mechanisms of exocytosis and endocytotic, as they are in the clinical treatment of dystonias. Expand


Botulinum neurotoxin and tetanus toxin
Let's read! We will often find out this sentence everywhere. When still being a kid, mom used to order us to always read, so did the teacher. Some books are fully read in a week and we need theExpand
A Sourcebook ofBacterial Protein Toxins
  • 1991