Activation and Inactivation of Tetanus Toxin in Chromaffin Cells

Tetanus toxin is produced by Clostridium tetani as a single chain, almost non-toxic, protein with a molecular weight of approximately 150.000 representing 1315 amino acids. Bacterial proteases cleave the molecule between positions A 457 and S 458 (extracellular activation), yielding a heavy chain (MW 100.000) and a light chain (MW 50.000) tetanus toxin (HC-TeTx, LC-TeTx). Both chains remain connected to each other by a disulphur bond between positions C 439 and C 467 (Dichain-TeTx)1. The cleavage or nicking dramatically increases the biological activity2. HC-TeTx is involved in binding DC-TeTx to gangliosides lodged in the plasma membrane, which is a prerequisite for incorporation into the …