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
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Toxins / chemistry*
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Bacterial Toxins / metabolism
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Clostridium perfringens / genetics
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Diethyl Pyrocarbonate / chemistry
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Hemolysin Proteins
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Histidine / chemistry*
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Liposomes / metabolism
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Macromolecular Substances
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Spectrometry, Fluorescence
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Tryptophan / chemistry
Substances
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Bacterial Toxins
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Hemolysin Proteins
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Liposomes
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Macromolecular Substances
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Histidine
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Clostridium perfringens theta-toxin
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Tryptophan
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Diethyl Pyrocarbonate