Contribution of histidine residues to oligomerization of theta-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.
Nakamura
M
M
Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan. megumi@tmig.or.jp
Sekino-Suzuki
N
N
Shimada
Y
Y
Ohno-Iwashita
Y
Y
D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D003016:Clostridium perfringens / Q000235:genetics; D004047:Diethyl Pyrocarbonate / Q000737:chemistry; D006460:Hemolysin Proteins; D006639:Histidine / Q000737:chemistry*; D008081:Liposomes / Q000378:metabolism; D046911:Macromolecular Substances; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry
D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D008081:Liposomes; D046911:Macromolecular Substances; D006639:Histidine; C020452:Clostridium perfringens theta-toxin; D014364:Tryptophan; D004047:Diethyl Pyrocarbonate