Hemolytic and sphingomyelinase activities of Clostridium perfringens alpha-toxin are dependent on a domain homologous to that of an enzyme from the human arachidonic acid pathway.
The N-terminal domain of Clostridium perfringens alpha-toxin, homologous with the nontoxic phospholipase C of Bacillus cereus, was expressed in Escherichia coli and shown to retain all of the phosphatidylcholine hydrolyzing activity of the alpha-toxin, but not the sphingomyelinase, hemolytic, or lethal activities. The C-terminal domain of alpha-toxin showed sequence and predicted structural homologies with the N-terminal region of arachidonate 5-lipoxygenase, an enzyme from the human arachidonic acid pathway which plays a role in inflammatory and cardiovascular diseases in humans.
Titball
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Chemical Defence Establishment, Salisbury, Wiltshire, United Kingdom.
Leslie
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Harvey
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Kelly
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D000595:Amino Acid Sequence; D016718:Arachidonic Acid; D001095:Arachidonic Acids / Q000378:metabolism*; D001427:Bacterial Toxins / Q000737:chemistry*; D002135:Calcium-Binding Proteins; D003016:Clostridium perfringens / Q000378:metabolism*; D006461:Hemolysis / Q000187:drug effects*; D006801:Humans; D008969:Molecular Sequence Data; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism*; D013329:Structure-Activity Relationship; D010738:Type C Phospholipases
D001095:Arachidonic Acids; D001427:Bacterial Toxins; D002135:Calcium-Binding Proteins; D016718:Arachidonic Acid; D010738:Type C Phospholipases; D013108:Sphingomyelin Phosphodiesterase; C040649:alpha toxin, Clostridium perfringens