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rat synaptobrevin 2 + H2O
?
-
catalytic activity of all mutants
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
vesicle associated membrane protein + H2O
?
vesicle associated membrane protein 1 + H2O
?
-
-
-
-
?
vesicle associated membrane protein 2 + H2O
?
vesicle associated membrane protein-1 + H2O
?
-
-
-
-
?
vesicle associated membrane protein-2 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein VAMP + H2O
?
vesicle-associated membrane protein-2 + H2O
?
-
neuronal SNARE protein, i.e. VAMP2
-
-
?
additional information
?
-
synaptobrevin + H2O
?
-
-
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
tetanus neurotoxin receptors are located on the motor neuron plasmalemma at neuromuscular junction, after binding the toxin is internalized inside vesicles of unknown nature and then translocated across the vesicle membrane
-
-
?
synaptobrevin + H2O
?
-
i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol
-
-
?
synaptobrevin + H2O
?
-
enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known
-
-
?
synaptobrevin + H2O
?
-
neurotoxin blocks neurotransmitter release in Aplysia neurons
-
-
?
synaptobrevin + H2O
?
-
TeNT is a zinc metalloprotease, that is produced by anaerobically grown Clostridium tetani in infected tissue, where it binds to ganglioside receptors of peripheral nerves. TeNT is then endocytosed. The A subunit exits from the endosome and undergoes retrograde transport via the nerve axon to the spinal cord of the host, where it specifically cleaves one of the nerve cell SNARE proteins, synaptobrevin
-
-
?
synaptobrevin + H2O
?
-
a host nerve cell SNARE protein, purified recombinant His-tagged synaptobrevin expressed in Escherichia coli
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known
-
-
?
synaptobrevin + H2O
?
-
-
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
-
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
i.e. VAMP, neuronal vesicle-associated membrane protein, MW 19000, with 2 isoforms in human, chicken, in rat brain: synaptobrevin/VAMP-1 and synaptobrevin/VAMP-2, cleaves at Gln76-Phe77, the same site as botulin neurotoxin B
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
i.e. VAMP, neuronal vesicle-associated membrane protein, MW 19000, with 2 isoforms in human, chicken, in rat brain: synaptobrevin/VAMP-1 and synaptobrevin/VAMP-2, cleaves at Gln76-Phe77, the same site as botulin neurotoxin B
-
-
?
synaptobrevin-2 + H2O
?
-
i.e. vesicle associated membrane protein-2, VAMP-2
-
-
?
synaptobrevin-2 + H2O
?
-
i.e. vesicle associated membrane protein-2, VAMP-2, or Syb2, specific proteolytic cleavage, development of a sensitive in vitro assay method using immobilized recombinant substrate and a highly specific polyclonal antibody against the newly generated C-terminus of the product, overview
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle associated membrane protein 2 + H2O
?
-
-
-
-
?
vesicle associated membrane protein 2 + H2O
?
-
preferred substrate
-
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
-
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
L-chain highly specific for the substrate
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
L-chain highly specific for the substrate
-
?
additional information
?
-
-
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
-
-
?
additional information
?
-
-
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
-
-
?
additional information
?
-
-
catalytic activity requires reduction of the single interchain disulfide bond of the neurotoxin
-
-
?
additional information
?
-
-
no substrates are rat or chicken
-
-
?
additional information
?
-
-
no substrates are rat or chicken
-
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
additional information
?
-
-
most powerful known natural toxin, 2 carbohdrate binding sites in the Hcc-domain of tetanus neurotoxin are required for toxicity
-
?
additional information
?
-
-
most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords
-
?
additional information
?
-
-
tetanus neurotoxin is a potent inhibitor of neuroexocytosis. Organization and regulation of the neurotoxin gene. The gene located immediately upstream of the tetanus toxin gene, encodes a positive regulatory protein, TetR
-
-
?
additional information
?
-
-
TeNT high affinity binding to neurons is mediated solely by its gangliosides, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells. Gangliosides are functional dual receptors for TeNT, overview
-
-
?
additional information
?
-
-
the conformational changes of the C fragment of tetanus neurotoxin (TeNTHc) resulting from disulfide bond formation reduce the ganglioside-binding activity but do not destroy its immunogenicity as a potent vaccine candidate
-
-
?
additional information
?
-
-
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
-
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synaptobrevin-2 + H2O
?
-
i.e. vesicle associated membrane protein-2, VAMP-2
-
-
?
vesicle associated membrane protein + H2O
?
vesicle associated membrane protein 1 + H2O
?
-
-
-
-
?
vesicle associated membrane protein 2 + H2O
?
vesicle associated membrane protein-1 + H2O
?
-
-
-
-
?
vesicle associated membrane protein-2 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
neuronal SNARE protein, i.e. VAMP2
-
-
?
additional information
?
-
synaptobrevin + H2O
?
-
-
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
tetanus neurotoxin receptors are located on the motor neuron plasmalemma at neuromuscular junction, after binding the toxin is internalized inside vesicles of unknown nature and then translocated across the vesicle membrane
-
-
?
synaptobrevin + H2O
?
-
i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol
-
-
?
synaptobrevin + H2O
?
-
enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known
-
-
?
synaptobrevin + H2O
?
-
neurotoxin blocks neurotransmitter release in Aplysia neurons
-
-
?
synaptobrevin + H2O
?
-
TeNT is a zinc metalloprotease, that is produced by anaerobically grown Clostridium tetani in infected tissue, where it binds to ganglioside receptors of peripheral nerves. TeNT is then endocytosed. The A subunit exits from the endosome and undergoes retrograde transport via the nerve axon to the spinal cord of the host, where it specifically cleaves one of the nerve cell SNARE proteins, synaptobrevin
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known
-
-
?
synaptobrevin + H2O
?
-
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle associated membrane protein 2 + H2O
?
-
-
-
-
?
vesicle associated membrane protein 2 + H2O
?
-
preferred substrate
-
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
additional information
?
-
-
most powerful known natural toxin, 2 carbohdrate binding sites in the Hcc-domain of tetanus neurotoxin are required for toxicity
-
?
additional information
?
-
-
most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords
-
?
additional information
?
-
-
tetanus neurotoxin is a potent inhibitor of neuroexocytosis. Organization and regulation of the neurotoxin gene. The gene located immediately upstream of the tetanus toxin gene, encodes a positive regulatory protein, TetR
-
-
?
additional information
?
-
-
TeNT high affinity binding to neurons is mediated solely by its gangliosides, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells. Gangliosides are functional dual receptors for TeNT, overview
-
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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The complete nucleotide sequence of tetanus toxin
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14
7809-7813
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Clostridium tetani
brenda
Rossetto, O.; Schiavo, G.; Polverino de Laureto, P.; Fabbiani, S.; Montecucco, C.
Surface topography of histidine residues of tetanus toxin probed by immobilized-metal-ion affinity chromatography
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Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins
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Schiavo, G.; Benfenati, F.; Poulain, B.; Rossetto, O.; Polverino de Laureto, P.; DasGupta, B.R.; Montecucco, C.
Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
Nature
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Montecucco, C.; Schiavo, G.
Mechanism of action of tetanus and botulinum neurotoxins
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13
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1994
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Schiavo, G.; Montecucco, C.
Tetanus and botulism neurotoxins: isolation and assay
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1995
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Umland, T.C.; Wingert, L.; Swaminathan, S.; Schmidt, J.J.; Sax, M.
Crystallization and preliminary X-ray analysis of tetanus neurotoxin C fragment
Acta Crystallogr. Sect. D
54
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Clostridium tetani
brenda
Meneghini, C.; Morante, S.
The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy
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75
1953-1963
1998
Clostridium tetani
brenda
Sutton, J.M.; Chow-Worn, O.; Spaven, L.; Silman, N.J.; Hallis, B.; Shone, C.C.
Tyrosine-1290 of tetanus neurotoxin plays a key role in its binding to gangliosides and functional binding to neurones
FEBS Lett.
493
45-49
2001
Clostridium tetani
brenda
Rummel, A.; Bade, S.; Alves, J.; Bigalke, H.; Binz, T.
Two carbohydrate binding sites in the H(CC)-domain of tetanus neurotoxin are required for toxicity
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2003
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Tonello, F.; Pellizzari, R.; Pasqualato, S.; Grandi, G.; Peggion, E.; Montecucco, C.
Recombinant and truncated tetanus neurotoxin light chain: cloning, expression, purification, and proteolytic activity
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15
221-227
1999
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Brueggemann, H.; Gottschalk, G.
Insights in metabolism and toxin production from the complete genome sequence of Clostridium tetani
Anaerobe
10
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2004
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Raffestin, S.; Marvaud, J.C.; Cerrato, R.; Dupuy, B.; Popoff, M.R.
Organization and regulation of the neurotoxin genes in Clostridium botulinum and Clostridium tetani
Anaerobe
10
93-100
2004
Clostridium tetani
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Fratelli, F.; Siquini, T.J.; Prado, S.M.; Higashi, H.G.; Converti, A.; de Carvalho, J.C.
Effect of medium composition on the production of tetanus toxin by Clostridium tetani
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21
756-761
2005
Clostridium tetani
brenda
Rao, K.N.; Kumaran, D.; Binz, T.; Swaminathan, S.
Structural analysis of the catalytic domain of tetanus neurotoxin
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45
929-939
2005
Clostridium tetani (P04958)
brenda
Kegel, B.; Behrensdorf-Nicol, H.A.; Bonifas, U.; Silberbach, K.; Klimek, J.; Kraemer, B.; Weisser, K.
An in vitro assay for detection of tetanus neurotoxin activity: Using antibodies for recognizing the proteolytically generated cleavage product
Toxicol. in Vitro
21
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2007
Clostridium tetani
brenda
Indrawattana, N.; Sookrung, N.; Kulkeaw, K.; Seesuay, W.; Kongngoen, T.; Chongsa-nguan, M.; Tungtrongchitr, A.; Chaicumpa, W.
Human monoclonal ScFv that inhibits cellular entry and metalloprotease activity of tetanus neurotoxin
Asian Pac. J. Allergy Immunol.
28
85-93
2010
Clostridium tetani
brenda
Chen, C.; Fu, Z.; Kim, J.J.; Barbieri, J.T.; Baldwin, M.R.
Gangliosides as high affinity receptors for tetanus neurotoxin
J. Biol. Chem.
284
26569-26577
2009
Clostridium tetani
brenda
Yu, R.; Yi, S.; Yu, C.; Fang, T.; Liu, S.; Yu, T.; Song, X.; Fu, L.; Hou, L.; Chen, W.
A conformational change of C fragment of tetanus neurotoxin reduces its ganglioside-binding activity but does not destroy its immunogenicity
Clin. Vaccine Immunol.
18
1668-1672
2011
Clostridium tetani
brenda
Behrensdorf-Nicol, H.A.; Weisser, K.; Kraemer, B.
"BINACLE" assay for in vitro detection of active tetanus neurotoxin in toxoids
ALTEX
32
137-142
2015
Clostridium tetani
brenda
Watanabe, Y.; Matsuba, T.; Nakanishi, M.; Une, M.; Hanajima, R.; Nakashima, K.
Tetanus toxin fragments and Bcl-2 fusion proteins cytoprotection and retrograde axonal migration
BMC Biotechnol.
18
39
2018
Clostridium tetani, Clostridium tetani KZ1174
brenda
Ferecsko, A.; Jiruska, P.; Foss, L.; Powell, A.; Chang, W.; Sik, A.; Jefferys, J.
Structural and functional substrates of tetanus toxin in an animal model of temporal lobe epilepsy
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220
1013-1029
2015
Clostridium tetani
-
brenda
Rossetto, O.; Pirazzini, M.; Lista, F.; Montecucco, C.
The role of the single interchains disulfide bond in tetanus and botulinum neurotoxins and the development of antitetanus and antibotulism drugs
Cell. Microbiol.
21
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2019
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Torabi Goudarzi, S.; Hajivalili, M.; Hosseini, M.; Ghafari Khamene, M.; Yazdani, Y.; Sadreddini, S.; Miahipour, A.; Younesi, V.; Yousefi, M.
Tetanus neurotoxin HCC protein commits T cells to IFN-gamma producing cells
Cell. Mol. Biol.
62
20-24
2016
Clostridium tetani
brenda
Masuyer, G.; Conrad, J.; Stenmark, P.
The structure of the tetanus toxin reveals pH-mediated domain dynamics
EMBO Rep.
18
1306-1317
2017
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Zuverink, M.; Chen, C.; Przedpelski, A.; Blum, F.; Barbieri, J.
A heterologous reporter defines the role of the tetanus toxin interchain disulfide in light-chain translocation
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2015
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Nagoba, B.; Dharne, M.; Gohil, K.N.
Molecular methods for identification of Clostridium tetani by targeting neurotoxin
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2017
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Khalili, E.; Lakzaei, M.; Rasaee, M.J.; Aminian, M.
Production of Recombinant human scFv against tetanus toxin heavy chain by phage display technology
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Epitope mapping of tetanus toxin by monoclonal antibodies implication for immunotherapy and vaccine design
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37
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2019
Clostridium tetani
brenda
Moeller, J.; Kraner, M.E.; Burkovski, A.
More than a toxin Protein inventory of Clostridium tetani toxoid vaccines
Proteomes
7
15
2019
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brenda
Pirazzini, M.; Azarnia Tehran, D.; Zanetti, G.; Rossetto, O.; Montecucco, C.
Hsp90 and thioredoxin-thioredoxin reductase enable the catalytic activity of Clostridial neurotoxins inside nerve terminals
Toxicon
147
32-37
2018
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brenda
Surana, S.; Tosolini, A.P.; Meyer, I.F.G.; Fellows, A.D.; Novoselov, S.S.; Schiavo, G.
The travel diaries of tetanus and botulinum neurotoxins
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147
58-67
2018
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brenda
Bano, L.; Tonon, E.; Drigo, I.; Pirazzini, M.; Guolo, A.; Farina, G.; Agnoletti, F.; Montecucco, C.
Detection of Clostridium tetani neurotoxins inhibited in vivo by botulinum antitoxin B Potential for misleading mouse test results in food controls
Toxins
10
248
2018
Clostridium tetani, Clostridium tetani ATCC 10779, Clostridium tetani TV1277
brenda
Wang, H.; Yu, R.; Fang, T.; Yu, T.; Chi, X.; Zhang, X.; Liu, S.; Fu, L.; Yu, C.; Chen, W.
Tetanus neurotoxin neutralizing antibodies screened from a human immune scFv antibody phage display library
Toxins
8
266
2016
Clostridium tetani
brenda
Carle, S.; Pirazzini, M.; Rossetto, O.; Barth, H.; Montecucco, C.
High conservation of tetanus and botulinum neurotoxins cleavage sites on human SNARE proteins suggests that these pathogens exerted little or no evolutionary pressure on humans
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9
404
2017
Clostridium tetani
brenda
Behrensdorf-Nicol, H.A.; Kraemer, B.
Is the test for irreversibility of tetanus toxoids still relevant?
Vaccine
37
1721-1724
2019
Clostridium tetani
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