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Tetanus toxin
Tetanus toxin (TeNT) is an extremely potent neurotoxin produced by the vegetative cell of Clostridium tetani in anaerobic conditions, causing tetanus. It has no known function for clostridia in the soil environment where they are normally encountered. It is also called spasmogenic toxin, tentoxilysin, tetanospasmin, or tetanus neurotoxin. The LD50 of this toxin has been measured to be approximately 2.5–3 ng/kg, making it second only to the related botulinum toxin (LD50 2 ng/kg) as the deadliest toxin in the world. However, these tests are conducted solely on mice, which may react to the toxin differently from humans and other animals.
C. tetani also produces the exotoxin tetanolysin, a hemolysin, that causes destruction of tissues.
Tetanus toxin spreads through tissue spaces into the lymphatic and vascular systems. It enters the nervous system at the neuromuscular junctions and migrates through nerve trunks and into the central nervous system (CNS) by retrograde axonal transport by using dyneins.
The tetanus toxin protein has a molecular weight of 150 kDa. It is translated from the tetX gene as one protein which is subsequently cleaved into two parts: a 100 kDa heavy or B-chain and a 50 kDa light or A-chain. The chains are connected by a disulfide bond.
The TetX gene encoding this protein is located on the PE88 plasmid.
Several structures of the binding domain and the peptidase domain have been solved by X-ray crystallography and deposited in the PDB.
The mechanism of TeNT action can be broken down and discussed in these different steps:
The first three steps outline the travel of tetanus toxin from the peripheral nervous system to where it is taken up to the CNS and has its final effect. The last three steps document the changes necessary for the final mechanism of the neurotoxin.
Tetanus toxin
Tetanus toxin (TeNT) is an extremely potent neurotoxin produced by the vegetative cell of Clostridium tetani in anaerobic conditions, causing tetanus. It has no known function for clostridia in the soil environment where they are normally encountered. It is also called spasmogenic toxin, tentoxilysin, tetanospasmin, or tetanus neurotoxin. The LD50 of this toxin has been measured to be approximately 2.5–3 ng/kg, making it second only to the related botulinum toxin (LD50 2 ng/kg) as the deadliest toxin in the world. However, these tests are conducted solely on mice, which may react to the toxin differently from humans and other animals.
C. tetani also produces the exotoxin tetanolysin, a hemolysin, that causes destruction of tissues.
Tetanus toxin spreads through tissue spaces into the lymphatic and vascular systems. It enters the nervous system at the neuromuscular junctions and migrates through nerve trunks and into the central nervous system (CNS) by retrograde axonal transport by using dyneins.
The tetanus toxin protein has a molecular weight of 150 kDa. It is translated from the tetX gene as one protein which is subsequently cleaved into two parts: a 100 kDa heavy or B-chain and a 50 kDa light or A-chain. The chains are connected by a disulfide bond.
The TetX gene encoding this protein is located on the PE88 plasmid.
Several structures of the binding domain and the peptidase domain have been solved by X-ray crystallography and deposited in the PDB.
The mechanism of TeNT action can be broken down and discussed in these different steps:
The first three steps outline the travel of tetanus toxin from the peripheral nervous system to where it is taken up to the CNS and has its final effect. The last three steps document the changes necessary for the final mechanism of the neurotoxin.
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