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Information on EC 3.4.24.68 - tentoxilysin and Organism(s) Clostridium tetani and UniProt Accession P04958
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3.4.24.68 tentoxilysinSpecify your search results
Word Map
- 3.4.24.68
- synaptic
- botulinum
- toxoid
- nerve
- epitope
-
neurotransmitter
-
exocytosis
- spinal
- ganglioside
- tetany
- cord
-
clostridial
-
retrograde
-
presynaptic
- synaptobrevin
- snare
- antitoxin
- epilepsy
- neuromuscular
-
transmitter
- synapses
- diphtheria
-
excitatory
-
bonts
-
vesicle-associated
- snap-25
- syntaxin
-
postsynaptic
- paralysis
- vamp
- motoneuron
-
synaptosomes
- gt1b
-
booster
-
n-ethylmaleimide-sensitive
-
toxin-induced
-
v-snares
-
intrahippocampal
-
transsynaptic
-
phrenic
-
neuroparalytic
-
holotoxin
-
k+-evoked
-
neurospecific
-
electrograph
-
monosynaptic
-
circumsporozoite
-
synaptosome-associated
- medicine
-
interictal
-
3hnoradrenaline
The taxonomic range for the selected organisms is: Clostridium tetani
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
Synonyms
tetanus toxin, tetanus neurotoxin, tetanospasmin, tent-hc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TeNT
-
-
Tentoxylysin
-
-
-
-
Tetanus neurotoxin
Tetanus neurotoxin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
structure and mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
107231-12-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rat synaptobrevin 2 + H2O
?
-
catalytic activity of all mutants
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
L-chain highly specific for the substrate
-
?
vesicle-associated membrane protein-2 + H2O
?
-
neuronal SNARE protein, i.e. VAMP2
-
-
?
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
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
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
synaptobrevin-2 + H2O
?
-
i.e. vesicle associated membrane protein-2, VAMP-2
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
neuronal SNARE protein, i.e. VAMP2
-
-
?
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zinc
Zn2+
Zn2+
crystal structure provides insight into the role of the zinc ion
Zinc
-
1 atom zinc per molecule toxin, zinc-binding motif: His-Glu-X-X-His, nickel or cobalt can replace zinc
Zinc
-
L-chain: form of zinc-endopeptidase, 0.8-1 gatom zinc/mol toxin, bound to light or L-chain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ala-Ser-Gln-Phe-Glu-Thr-Ser
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica
Gln-Phe-Glu-Thr
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica
additional information
-
enzyme inhibition by a cleavage site-specific antibody, overview
-
additional information
-
design, random selection, and recombinant production from phagemid in Escherichia coli of human single chain antibody fragments that inhibit tetanus toxin binding to retinoic acid pulsed human neuroblastoma cells and TeNT protease activity completely, overview
-
additional information
-
geldanamycin efficiently blocks the neurotoxic activity of the enzyme. The interchain disulfide of the enzyme can be specifically reduced by incubating the enzyme with NADPH, thioredoxin and thioredoxin reductase. Reduced enzyme is not toxic
-
additional information
-
not inhibited by botulinum antitoxin types A, C, D, E and F
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Proteases
-
activation by rapid cleavage within an exposed loop of the single inactive MW 150000 polypeptide chain and generation of active di-chain neurotoxin
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
in neurotoxin-injected Aplysia neurons 4-10 molecules of L-chains are sufficient to cause blockade of neurotransmitter release with a t1/2 of 20-40 min at 20°C
additional information
-
quantitative immunoaffinity assay method development and evaluation, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
effect of medium composition on the production of tetanus toxin. The highest final average yield of tetanus toxin is obtained at 9.7 mg/ml starting level of glucose and 43.5 g/l N-T Case TT as carbon and nitrogen source
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
TeNT cleaves vesicle-associated membrane protein-2, thereby inhibiting neurotransmitter release in the central nervous system to elicit spastic paralysis
metabolism
-
the enzyme cleaves a neuronal soluble N-ethylmaleimide-sensitive attachment receptor protein, leading to the blockade of inhibitory neurotransmitter release and subsequent generalized muscular spasm
physiological function
physiological function
-
cleavage of synaptobrevin results in inhibition of release of neurotransmitters glycine and gamma-amino butyric acid from inhibitory interneurons causing spastic paralysis
physiological function
-
the enzyme is the most important virulence factor that plays a key role in the pathogenicity of tetanus
physiological function
-
the enzyme undergoes binding to specific components of the basal membrane at the neuromuscular junction, is endocytosed into motor neurons and sorted to axonal signaling endosomes. Following this, the enzyme is transported to the soma of motor neurons located in the spinal cord or brainstem, and then transcytosed to inhibitory interneurons, where it blocks synaptic transmission. Enzyme-induced impairment of inhibitory input leads to hyperactivity of motor neurons, causing spastic paralysis
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
1 * 100000, C-terminal heavy chain, + 1 * 50000, N-terminal light chain
150000
50000
-
1 * 100000, C-terminal heavy chain, + 1 * 50000, N-terminal light chain
additional information
-
amino acid sequence homologies between tetanus toxin TeNT and botulinum toxins BoNT/A, B and E
150000
-
activated by proteolytic cleavage with formation of a 50 kDa L-chain and a 100 kDa H-chain
150000
-
single-chain protein, cleaved by proteases into a 100 kDa heavy chain HC and a 50 kDa light chain LC, SELDI-TOF MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
1 * 100000, C-terminal heavy chain, + 1 * 50000, N-terminal light chain
additional information
additional information
-
the enzyme consists of a heavy (H) chain and a light (L) chain
additional information
-
the enzyme consists of a heavy (H) chain and a light (L) chain
additional information
-
held together by a single disulfide bond and non-covalent forces
additional information
-
MW 52288 (L-chain) and MW 98300 (H-chain), calculated from amino acid sequence
additional information
-
TeNT is an A-B toxin. It consits of a heavy chain containing cellular receptor binding domain and a light chain with zinc metalloprotease activity
additional information
-
the TeNT heavy chain contains two functional domains: a translocation domain and a C-terminal receptor binding domain. C-terminal heavy and N-terminal light chains are linked through a single disulfide bond, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycolipoprotein
-
gangliosides are bound to the C-terminal receptor-binding domain via two carbohydrate-binding sites, termed the lactose-binding site or the W pocket, and the sialic acid-binding site or the R pocket, GM1a bound to the W pocket, and GD3 bound to the R pocket
proteolytic modification
-
TeNT is produced as a 150-kDa protein that is cleaved to a di-chain protein, comprising an N-terminal light chain and a C-terminal heavy chain domain linked through a single disulfide bond
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ganglioside GD1a, hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3350, 0.1xa0M Bis-Tris propane pH 6.5, 0.2xa0M potassium thiocyanate. In complex with ganglioside GM1a, sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1xa0M MES pH 6.0, 0.2xa0M sodium chloride
sitting drop vapor diffusion method. The structure provides insight into the active site, the importance of the nucleophilic water and the role of the zinc ion
purified C-terminal receptor binding domain with bound ganglioside GT2 in presence and absence of lactose, 10 mg/ml protein in 20 mM Tris-HCl buffer, pH 7.9, containing 100 mM NaCl are mixed with the carbohydrate moiety of GT2 at 1:8 molar ratio, vapor diffusion hanging drop method, 0.002 ml of protein-ligand solution are mixed with 0.002 ml of well solution containing 100 mM bis(trispropane) buffer, pH 7.0, 25% polyethylene glycol 2000 and 300 mM ammonium sulfate, equilibration against 0.5 ml well solution at 19°C, X-ray diffraction structure determination and analysis at 2.0-2.1 A resolution, molecular replacement method
-
tetanus neurotoxin C fragment, vapor-diffusion method, hanging drops and sitting drops, thick rod-shaped crystals, space group P2(1)2(1)2(1), unit cell dimensions a : 67.4 A, b : 79.7 A, c : 91.1 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R372A/Y375F
-
the enzyme activity is about125,000fold reduced in toxicity relative to native protein
Y1290F
additional information
-
construction of mutated forms of HCR/T that lack one or both carbohydrate-binding pocket, loss of gangliosides binding ability leads to loss of neuron binding ability of the toxin, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, in 10 mM HEPES buffer, pH 7.2, 50 mM NaCl, after freezing in liquid N2, stable
-
37°C, enzyme diluted in water supplemented with 5 mg/ml protease-free bovine serum albumin, 3 days, 90% loss of activity
-
37°C, enzyme diluted in water supplemented with 5 mg/ml protease-free bovine serum albumin, 35-45 days, complete loss of activity
-
4°C, both native and recombinant TeNT L-chains show significant decreases after 3-4 days of storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
very toxic! Booster injection of tetanus toxoid before starting research with tetanus toxin advisable, human anti-tetanus neurotoxin antibodies available
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM101 using three different plasmid vectors
-
mutant enzyme R372A/Y375F fused to beta-lactamase, expressed in Escherichia coli BL21(DE3) cells
-
the C-terminal domain bound to Bcl-2 protein is expressed in COS-7 cells and Escherichia coli BL21(DE3)pLysS cells
-
the heavy chain fragment is expressed in Escherichia coli BL21(DE3) cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
sole causal agent of the pathological condition known as tetanus
medicine
-
very powerful neurotoxin, agent responsible for all clinical symptoms of tetanus
medicine
-
HuscFv antibodies specific for heavy chain can protect against tetanus neurotoxin by inhibiting binding of the enzyme to ganglioside GT1b
medicine
-
monoclonal antibody MAb 5C4 is the only anti-fragment C (heavy chain) antibody which is capable of blocking the binding of recombinant fragment C to GT1b gangliosides
medicine
-
the antibodies 2-7G, 2-2D, and S-4-7H can effectively inhibit the binding between the heavy chain fragment of the enzyme (TeNT-Hc) and differentiated PC-12 cells in vitro. Moreover, 2-7G inhibits TeNT-Hc binding to the receptor via carbohydrate-binding sites of the W pocket while 2-2D and S-4-7H inhibit binding of the R pocket. Although no single antibody completely protect mice from the toxin, they can prolong survival
medicine
-
treatment of T cells with recombinant carboxy-subdomain of the heavy chain results in development of Th1 lineage phenotype, which might lead to a specific and protective antibody mediated response against the enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fairweather, N.F.; Lyness, V.A.
The complete nucleotide sequence of tetanus toxin
Nucleic Acids Res.
14
7809-7813
1986
Clostridium tetani
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
Biochem. J.
285
9-12
1992
Clostridium tetani
Eisel, U.; Jarusch, W.; Goretzki, K.; Henschen, A.; Engels, J.; Weller, U.; Hudel, M.; Habermann, E.; Niemann, H.
Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins
EMBO J.
5
2495-2502
1986
Clostridium tetani
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
359
832-835
1992
Clostridium tetani
Montecucco, C.; Schiavo, G.
Mechanism of action of tetanus and botulinum neurotoxins
Mol. Microbiol.
13
1-8
1994
Clostridium tetani
Schiavo, G.; Montecucco, C.
Tetanus and botulism neurotoxins: isolation and assay
Methods Enzymol.
248
643-652
1995
Clostridium tetani, Clostridium tetani Harvard
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
273-275
1998
Clostridium tetani
Meneghini, C.; Morante, S.
The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy
Biophys. J.
75
1953-1963
1998
Clostridium tetani
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
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
J. Mol. Biol.
326
835-847
2003
Clostridium tetani
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
Protein Expr. Purif.
15
221-227
1999
Clostridium tetani, Clostridium tetani Y-IV-3
Brueggemann, H.; Gottschalk, G.
Insights in metabolism and toxin production from the complete genome sequence of Clostridium tetani
Anaerobe
10
53-68
2004
Clostridium tetani (Q93N27), Clostridium tetani
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
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
Biotechnol. Prog.
21
756-761
2005
Clostridium tetani
Rao, K.N.; Kumaran, D.; Binz, T.; Swaminathan, S.
Structural analysis of the catalytic domain of tetanus neurotoxin
Toxicon
45
929-939
2005
Clostridium tetani (P04958)
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
1641-1649
2007
Clostridium tetani
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
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
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
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
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
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
Brain Struct. Funct.
220
1013-1029
2015
Clostridium tetani
-
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
e13037
2019
Clostridium tetani
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
Masuyer, G.; Conrad, J.; Stenmark, P.
The structure of the tetanus toxin reveals pH-mediated domain dynamics
EMBO Rep.
18
1306-1317
2017
Clostridium tetani (P04958), Clostridium tetani, Clostridium tetani E88 (P04958)
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
Infect. Immun.
83
2714-2724
2015
Clostridium tetani
Nagoba, B.; Dharne, M.; Gohil, K.N.
Molecular methods for identification of Clostridium tetani by targeting neurotoxin
Methods Mol. Biol.
1600
37-47
2017
Clostridium tetani
Khalili, E.; Lakzaei, M.; Rasaee, M.J.; Aminian, M.
Production of Recombinant human scFv against tetanus toxin heavy chain by phage display technology
Monoclon. Antib. Immunodiagn. Immunother.
34
303-309
2015
Clostridium tetani
Ghotloo, S.; Golsaz-Shirazi, F.; Amiri, M.M.; Jeddi-Tehrani, M.; Shokri, F.
Epitope mapping of tetanus toxin by monoclonal antibodies implication for immunotherapy and vaccine design
Neurotox. Res.
37
239-249
2019
Clostridium tetani
Moeller, J.; Kraner, M.E.; Burkovski, A.
More than a toxin Protein inventory of Clostridium tetani toxoid vaccines
Proteomes
7
15
2019
Clostridium tetani (P04958), Clostridium tetani, Clostridium tetani E88 (P04958)
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
Clostridium tetani
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
Toxicon
147
58-67
2018
Clostridium tetani
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
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
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
Toxins
9
404
2017
Clostridium tetani
EXTERNAL LINKS (specific for EC-Number 3.4.24.68)
Transporter Classification Database (TCDB): 1.C.8.1.2
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