Tetanus Toxin, C-Fragment

Tetanus Toxin, C-Fragment refers to the C-terminal binding component of the heavy chain derived from tetanus toxin, an infectious substance produced by the Gram-positive bacterium Clostridium tetani, found in soil and the gastrointestinal tracts of animals. Tetanus Toxin is a 150.7 kDa protein consisting of a 52.4 kDa light chain and a 98.3 kDa heavy chain connected by a disulfide bond. The heavy chain comprises fragments B and C, with fragment C weighing 51.6 kDa and positioned at the C-terminus, responsible for neuronal cell binding. The non-toxic nature, immunological attributes, and neuronal binding properties of the tetanus toxin fragment C (TTFC) have rapidly brought it into the spotlight. Thus, It serves as useful for binding studies. The tetanus toxin fragment C (TTFC) has garnered considerable attention due to its neurological properties in vitro. As a derivative of the tetanus toxin, it retains its immunogenic properties without toxicity. Moreover, TTFC has undergone extensive characterization, and its complete structure is known. Tetanus Toxin operates by inhibiting neurotransmitter release, leading to spastic paralysis through a four-step process. Firstly, Tetanus Toxin binds to specific receptors, predominantly composed of lipids and gangliosides, located at the neuromuscular junction. Additionally, Tetanus Toxin engages another receptor involved in its internalization, thereby establishing a strong affinity between Tetanus Toxin and nerve cells. Subsequently, Tetanus Toxin undergoes axonal retrograde transport to reach the cell body. Finally, Tetanus Toxin cleaves the VAMP/synaptobrevin, a neuronal substrate, via proteolysis, resulting in the inhibition of neurotransmitter release.