Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis.

@article{Iwamoto1990EffectOI,
  title={Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis.},
  author={Mari Iwamoto and Yoshiko Ohno-Iwashita and Sebastiano And{\`o}},
  journal={European journal of biochemistry},
  year={1990},
  volume={194 1},
  pages={25-31}
}
theta-toxin, a thiol-activated cytolysin, binds cholesterol and assembles on plasma membrane during the lytic process. In order to understand the process at the molecular level, two fragments (T1 and T2) were isolated from a nicked toxin obtained by limited proteolysis with trypsin. Although neither the T1 nor T2 fragment has hemolytic activity. T2 has almost the same potential as native theta-toxin in its binding affinity for erythrocytes and in its binding specificity for cholesterol. T2… CONTINUE READING