The C terminal binding portion of tetanus toxin is not toxic but is taken up by pre-synaptic nerve terminals and exhibits trans-synaptic retrograde transport in central neurons similar to that of tetanus toxin. It is used to map neuronal connections and to target proteins to neurons.
Tetanus toxin C fragment (TTC) is a non-toxic peptide, which is transported from peripheral axons into spinal motoneurons. It provides protection for motoneurons (MN) in the spinal cord in vivo. TTC regulates membrane binding, internalization and retrograde transport within MN. It initiates neurotrophin-regulated signaling pathways in a Trk receptor-dependent manner. TTC has neuroprotective property in primary cerebellar granule cell culture.
Tetanus toxin is a neurotoxin that comprises of a heavy and a light chain linked by disulfide bridges. This neurotoxin enters the cytoplasm and releases the light chain component that subsequently inhibits the release of neurotransmitters2. Studies have reported that the fragment C of tetanus toxin retains most of the determinants that interact with thyroid membranes, gangliosides and neural membranes3.
