The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins.
The heat shock protein Hsp90 is essential for uptake of the binary actin ADP-ribosylating toxins Clostridium perfringens iota-toxin and Clostridium difficile transferase into eukaryotic cells. Inhibition of Hsp90 by its specific inhibitor radicicol delayed intoxication of Vero cells by these toxins. A common Hsp90-dependent mechanism for their translocation is discussed.
Haug
Gerd
G
Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, D-79104 Freiburg, Germany.
Aktories
Klaus
K
Barth
Holger
H
D036002:ADP Ribose Transferases / Q000633:toxicity*; D000818:Animals; D001427:Bacterial Toxins / Q000633:toxicity*; D002522:Chlorocebus aethiops; D016360:Clostridioides difficile / Q000201:enzymology / Q000472:pathogenicity; D003016:Clostridium perfringens / Q000201:enzymology / Q000472:pathogenicity; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007783:Lactones / Q000494:pharmacology; D018942:Macrolides; D014709:Vero Cells
D001427:Bacterial Toxins; D018841:HSP90 Heat-Shock Proteins; D007783:Lactones; D018942:Macrolides; C050737:iota toxin, Clostridium perfringens; D036002:ADP Ribose Transferases; C035359:monorden