Contribution of histidine residues to oligomerization of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin

Biosci Biotechnol Biochem. 1999 Sep;63(9):1640-3. doi: 10.1271/bbb.63.1640.

Abstract

Theta-toxin (perfringolysin O) modified by diethyl pyrocarbonate, a histidine-specific reagent, lost its hemolytic activity. The modified toxin retains the activities of binding to and insertion into cholesterol-containing membranes but lacks the ability to form oligomers. These results suggest that histidine residues of theta-toxin contribute their share to cytolysis, especially the oligomerization process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / metabolism
  • Clostridium perfringens / genetics
  • Diethyl Pyrocarbonate / chemistry
  • Hemolysin Proteins
  • Histidine / chemistry*
  • Liposomes / metabolism
  • Macromolecular Substances
  • Spectrometry, Fluorescence
  • Tryptophan / chemistry

Substances

  • Bacterial Toxins
  • Hemolysin Proteins
  • Liposomes
  • Macromolecular Substances
  • Histidine
  • Clostridium perfringens theta-toxin
  • Tryptophan
  • Diethyl Pyrocarbonate