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|Title:||Clathrin-dependent trafficking of subtilase cytotoxin, a novel AB(5) toxin that targets the endoplasmic reticulum chaperone BiP|
|Citation:||Cellular Microbiology, 2008; 10(3):795-806|
|Publisher:||Blackwell Science Ltd|
|Damien C. Chong, James C. Paton, Cheleste M. Thorpe and Adrienne W. Paton|
|Abstract:||Subtilase cytotoxin (SubAB) is the prototype of a new family of AB5 cytotoxins produced by Shiga toxigenic Escherichia coli. Its cytotoxic activity is due to its capacity to enter cells and specifically cleave the endoplasmic reticulum (ER) chaperone BiP. However, its trafficking within target cells has not been investigated previously. In Vero cells, fluorescence colocalization with subcellular markers established that SubAB is trafficked from the cell surface to the ER via a retrograde pathway similar, but not identical, to those of Shiga toxin (Stx) and cholera toxin (Ctx), with their pathways converging at the Golgi. The clathrin inhibitor phenylarsine oxide prevented SubAB entry and BiP cleavage in SubAB-treated Vero, HeLa and N2A cells, while cholesterol depletion did not, demonstrating that, unlike either Stx or Ctx, SubAB internalization is exclusively clathrin-dependent.|
|Keywords:||Hela Cells; Vero Cells; Endoplasmic Reticulum; Golgi Apparatus; Animals; Cercopithecus aethiops; Humans; Arsenicals; Subtilisins; Escherichia coli Proteins; Heat-Shock Proteins; Clathrin; Molecular Chaperones; Enzyme Inhibitors; Microscopy, Fluorescence; Shiga-Toxigenic Escherichia coli|
|Description:||© 2008 Blackwell Publishing Ltd|
|Appears in Collections:||Molecular and Biomedical Science publications|
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