Role of processing and intracellular transport for optimal toxicity of Shiga toxin and toxin mutants.

@article{Garred1995RoleOP,
  title={Role of processing and intracellular transport for optimal toxicity of Shiga toxin and toxin mutants.},
  author={Oystein Garred and Elena Dubinina and Pontus Holm and Sjur Olsnes and Bo van Deurs and Juri V. Kozlov and Kirsten Sandvig},
  journal={Experimental cell research},
  year={1995},
  volume={218 1},
  pages={39-49}
}
Cleavage of Shiga toxin A-fragment at a highly trypsin-sensitive site increases its enzymatic activity. To investigate the role of this cleavage site in intoxication of cells, we studied the routing, cleavage, and toxicity of mutant toxin where the trypsin-sensitive site had been eliminated. Ultrastructural analysis of toxin tagged with horseradish peroxidase demonstrated that wild-type and mutant toxins were transported from endosomes to the trans-Golgi network and further through the Golgi… CONTINUE READING