Contribution of Histidine Residues to Oligomerization of θ-Toxin (Perfringolysin O), a Cholesterol-Binding Cytolysin
Copyright policy )Contribution of Histidine Residues to Oligomerization of θ-Toxin (Perfringolysin O), a Cholesterol-Binding Cytolysin
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.
Hemolysin Proteins, Spectrometry, Fluorescence, Clostridium perfringens, Macromolecular Substances, Bacterial Toxins, Diethyl Pyrocarbonate, Liposomes, Tryptophan, Histidine
Hemolysin Proteins, Spectrometry, Fluorescence, Clostridium perfringens, Macromolecular Substances, Bacterial Toxins, Diethyl Pyrocarbonate, Liposomes, Tryptophan, Histidine
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