Tetanus neurotoxin heavy chain fragment C (TTC)

Tetanus neurotoxin heavy chain fragment C (TTC) is the 50 kDa C-terminal domain of the tetanus toxin produced by Clostridium tetani [1]. It is primarily responsible for the toxin's specific recognition and binding to the presynaptic membranes of motor neurons, specifically targeting complex gangliosides like GD1b and GT1b [1, 3]. While the full tetanus toxin is a potent inhibitor of neurotransmitter release, Fragment C itself is non-toxic and retains the ability to undergo retrograde axonal transport from the periphery to the central nervous system [3]. This unique property makes it a critical component in the development of tetanus vaccines (toxoids) and a promising vehicle for the targeted delivery of therapeutic agents to the brain and spinal cord [3, 4]. In clinical practice, it is the primary antigen used to induce protective immunity against tetanus [2, 4]. Neutralizing antibodies generated against this fragment prevent the toxin from entering the nervous system, thereby preventing the clinical manifestations of tetanus [2]. Research also explores its use in neurobiology to map neuronal connections due to its highly specific uptake and transport mechanisms [3].

Other names

Tetanus toxin C-fragmentTeNT-HCFragment CTetanus toxin fragment C

Neutralization of toxin binding to neuronal membranes by inducing or providing specific antibodies that block the Fragment C domain [2, 4].