The heavy chain of tetanus toxin can mediate the entry of cytotoxic gelonin into intact cells

Johnstone, Stephen R.; Morrice, Lora M.; Heyningen, Simon van

doi:10.1016/0014-5793(90)80893-n

Cited by 8 publications

(2 citation statements)

References 13 publications

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“…These findings are in agreement with studies indicating that the heavy chain of tetanus toxin is involved in cell binding [41][42][43] in analogy to the closely related botulinum neurotoxins [44-463. These results indicate that, upon binding to the cell surface of this neuronal cell line, tetanus toxin interacts specifically and closely with a protein via its heavy chain. If a cross-linker is present, a covalent conjugate of about 120 kDa is formed.…”

Section: Immunoblottingsupporting

confidence: 92%

Tetanus toxin receptor Specific cross‐linking of tetanus toxin to a protein of NGF‐differentiated PC 12 cells

Schiavo¹,

Ferrari

Rossetto³

et al. 1991

FEBS Letters

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. In the presence of protein cross-linking agents, ['*'l]tetanus toxin, bound to these cells at O'C, forms a cross-linked product with apparent molecular weight of 120 kDa. The formation of ['*'I]tetanus toxin conjugate involves the heavy chain of the toxin, is prevented by cold toxin and it is largely reduced by pretreating cells with proteases. The cross-linked product is formed only upon incubation of the toxin with NGF-differentiated cells. These results suggest that a protein with apparent molecular weight of 20 kDa is involved in the neurospecific binding of tetanus toxin.

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Section: Immunoblottingsupporting

confidence: 92%

Tetanus toxin receptor Specific cross‐linking of tetanus toxin to a protein of NGF‐differentiated PC 12 cells

Schiavo¹,

Ferrari

Rossetto³

et al. 1991

FEBS Letters

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“…Clearly, more experiments are needed to clarify this mysterious third step of cell intoxication as well as the different membrane trafficking of TeNT and BoNT at the NMJ (see above section 5). A molecular understanding of such processes is a pre-requisite for the construction of vectors of biological reagents directed to neurons of the PNS and CNS, based on the H chains of the CNTs (Simpson, 1988;Johnstone et al 1990;Dobrenis et al 1992).…”

Section: Translocation Into the Neuronal Cytosolmentioning

confidence: 99%

Structure and function of tetanus and botulinum neurotoxins

Montecucco

Schiavo

1995

Quart. Rev. Biophys.

447

309

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Tetanus and botulinum neurotoxins are produced by Clostridia and cause the neuroparalytic syndromes of tetanus and botulism. Tetanus neurotoxin acts mainly at the CNS synapse, while the seven botulinum neurotoxins act peripherally. Clostridial neurotoxins share a similar mechanism of cell intoxication: they block the release of neurotransmitters. They are composed of two disulfide-linked polypeptide chains. The larger subunit is responsible for neurospecific binding and cell penetration. Reduction releases the smaller chain in the neuronal cytosol, where it displays its zinc-endopeptidase activity specific for protein components of the neuroexocytosis apparatus. Tetanus neurotoxin and botulinum neurotoxins B, D, F and G recognize specifically VAMP/ synaptobrevin. This integral protein of the synaptic vesicle membrane is cleaved at single peptide bonds, which differ for each neurotoxin. Botulinum A, and E neurotoxins recognize and cleave specifically SNAP-25, a protein of the presynaptic membrane, at two different sites within the carboxyl-terminus. Botulinum neurotoxin type C cleaves syntaxin, another protein of the nerve plasmalemma. These results indicate that VAMP, SNAP-25 and syntaxin play a central role in neuroexocytosis. These three proteins are conserved from yeast to humans and are essential in a variety of docking and fusion events in every cell. Tetanus and botulinum neurotoxins form a new group of zinc-endopeptidases with characteristic sequence, mode of zinc coordination, mechanism of activation and target recognition. They will be of great value in the unravelling of the mechanisms of exocytosis and endocytosis, as they are in the clinical treatment of dystonias.

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Clostridial Neurotoxins

Bigalke¹,

Shoer²

2000

Bacterial Protein Toxins

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The heavy chain of tetanus toxin can mediate the entry of cytotoxic gelonin into intact cells

Cited by 8 publications

References 13 publications

Tetanus toxin receptor Specific cross‐linking of tetanus toxin to a protein of NGF‐differentiated PC 12 cells

Tetanus toxin receptor Specific cross‐linking of tetanus toxin to a protein of NGF‐differentiated PC 12 cells

Structure and function of tetanus and botulinum neurotoxins

Clostridial Neurotoxins

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