Journal
CELLULAR MICROBIOLOGY
Volume 10, Issue 3, Pages 795-806Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1462-5822.2007.01085.x
Keywords
-
Categories
Funding
- NIAID NIH HHS [R01AI-068715, R01AI-59509] Funding Source: Medline
- NIDDK NIH HHS [P30DK-34928] Funding Source: Medline
Ask authors/readers for more resources
Subtilase cytotoxin (SubAB) is the prototype of a new family of AB(5) 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available