ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin.
The enzymatically active component ia of Clostridium perfringens iota toxin ADP-ribosylated actin in human platelet cytosol and purified platelet beta/gamma-actin, in a similar way to that been reported for component I of botulinum C2 toxin. ADP-ribosylation of cytosolic and purified actin by either toxin was inhibited by 0.1 mM phalloidin indicating that monomeric G-actin but not polymerized F-actin was the toxin substrate. Perfringens iota toxin and botulinum C2 toxin were not additive in ADP-ribosylation of platelet actin. Treatment of intact chicken embryo cells with botulinum C2 toxin decreased subsequent ADP-ribosylation of actin in cell lysates by perfringens iota or botulinum C2 toxin. In contrast to botulinum C2 toxin, perfringens iota toxin ADP-ribosylated skeletal muscle alpha-actin with a potency and efficiency similar to non-muscle actin. ADP-ribosylation of purified skeletal muscle and non-muscle actin by perfringens iota toxin led to a dose-dependent impairment of the ability of actin to polymerize.
D036002:ADP Ribose Transferases; D000199:Actins / Q000378:metabolism*; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism*; D001905:Botulinum Toxins / Q000378:metabolism*; D002478:Cells, Cultured; D002645:Chickens; D003016:Clostridium perfringens; D066298:In Vitro Techniques; D009132:Muscles / Q000378:metabolism; D010430:Pentosyltransferases / Q000378:metabolism; D011485:Protein Binding; D013379:Substrate Specificity
D000199:Actins; D001427:Bacterial Toxins; C050737:iota toxin, Clostridium perfringens; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; D010430:Pentosyltransferases; D001905:Botulinum Toxins