C-terminal half of tetanus toxin fragment C is sufficient for neuronal binding and interaction with a putative protein receptor

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C-terminal half of tetanus toxin fragment C is sufficient for neuronal binding and interaction with a putative protein receptor.

Tetanus neurotoxin (TeNT) is a powerful bacterial protein toxin that cleaves VAMP/synaptobrevin, an essential protein of the synaptic vesicle fusion machinery, and consequently blocks neurotransmission. The extreme neurospecificity of TeNT is determined by the binding of its C-terminal domain (fragment C or H(C)) to neuronal receptors. Whereas polysialogangliosides are known acceptors for the t...

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Cloning and expression of tetanus toxin C fragment (Fc) in prokaryotic vector for constructing recombinant protein based vaccine for tetanus

Tetanus is a disease caused by tetanus toxin, a potent inhibitor for the release of inhibitory neurotransmitter in the central nervous system that causes spastic paralysis. Fragment C (52 kD) of this toxin is responsible for binding to the neuronal membrane. For this reason, and also its non toxigenic and immunogenic nature, this fragment might be ideal for new vaccine development. Presently, w...

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Fragment C tetanus toxin: a putative activity-dependent neuroanatomical tracer.

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Immunogenic and Protective Potentials of Recombinant Receptor Binding Domain and a C-Terminal Fragment of Clostridium botulinum Neurotoxin Type E

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cloning and expression of tetanus toxin c fragment (fc) in prokaryotic vector for constructing recombinant protein based vaccine for tetanus

tetanus is a disease caused by tetanus toxin, a potent inhibitor for the release of inhibitory neurotransmitter in the central nervous system that causes spastic paralysis. fragment c (52 kd) of this toxin is responsible for binding to the neuronal membrane. for this reason, and also its non toxigenic and immunogenic nature, this fragment might be ideal for new vaccine development. presently, w...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2000

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3470199