Limited Proteolysis of Tetanus Toxin Light Chain by Trypsin at Its C-Terminus Causes a 10–30-Fold Decrease of Activity as Measured by Inhibition of Noradrenaline Release from Permeabilized Chromaffin Cells
The light chain (L) of tetanus toxin (TeTx) was shown to be the active principle of the inhibitory action of tetanus toxin in permeabilized cell systems, l,2 and if injected into neurons from Aplysia californica.3 It was shown to have the same activity as native toxin on a molar basis.1,3 Different L constructs expressed in E. coli and purified to homogeneity turned out to be proteolytically shortened at the C-terminus. Their activity in digitonin permeabilized chromaffin cells (PCC) was reduced to about 10% as compared with L from native toxin. CYS 438 was essential for activity in vivo but not in PCC.4
KeywordsLight Chain Limited Proteolysis Botulinum Neurotoxin Tetanus Toxin Native Toxin
Unable to display preview. Download preview PDF.
- 4.Weller U, Fairweather N, Sanders D, Ahnert-Hilger G, Payne M, Habermann E. Expression of tetanus toxin light chain and mutants of CYS 438 in E. coli: purification and biological activities of the recombinant proteins. Zbl Bakt Suppl 1992; 23: 99–100.Google Scholar
- 6.Binz T, Grebenstein O, Kurazono H, Eisel U, Wemars K, Popoff M, Mochida S, Poulain B, Tauc L, Kozaki S, Niemann H. Molecular biology of the L chains of clostridial neurotoxins. Zbl Bakt Suppl 1992; 23: 56–65.Google Scholar
- 8.Weller U, Dauzenroth M-E, Meyer zu Heringdorf D, Habermann E. Chains and fragments of tetanus toxin. Separation, reassociation and pharmacological properties. Eur J Biochem 1989; 182: 649–656.Google Scholar