File:Unfolded protein response to bacterial pore-forming toxins.png

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Unfolded_protein_response_to_bacterial_pore-forming_toxins.png(600 × 363 pixels, file size: 181 KB, MIME type: image/png)

Schematic illustrating relationship between p38 MAPK, ire-1-xbp-1, and Pore-forming toxins (PFTs) defense pathways

Pore-forming toxins (PFTs) at the cell surface of epithelial cells activate p38 MAPK that activates IRE-1 that induces splicing of xbp-1, which then turns on defense against PFTs. Residual activation of xbp-1 targets in the absence of the p38 MAPK pathway suggests there might be p38-independent activation of the ire-1-xbp-1 pathway in response to PFT as well (not shown). Independent of IRE-1 activation, p38 MAPK can also activate TTM-2 and other PFT defenses. Tunicamycin, which causes the accumulation of unfolded proteins in the ER, activates IRE-1 via a mechanism independent of the PFT and p38 MAPK.


Pore-forming toxins (PFTs) are the single most prevalent protein virulence factor made by disease-causing bacteria and are important for the virulence of many important human pathogens including Staphylococcus aureus, Streptococcus pyogenes, Clostridium perfringens, and Aeromonas hydrophilia [1],[2]. Crystal (Cry) toxins produced by the invertebrate pathogen Bacillus thuringiensis (Bt) are a large family of PFTs that target the intestinal cells of insects and nematodes.


The unfolded protein response (UPR) of the endoplasmic reticulum (ER) is a fundamental stress response used by eukaryotic cells to match protein synthesis demand to its capability to fold proteins within the ER to maintain cellular homeostasis

Figure 6. Journal.ppat.1000176.g006.png

Citation: Bischof LJ, Kao C-Y, Los FCO, Gonzalez MR, Shen Z, et al. (2008) Activation of the Unfolded Protein Response Is Required for Defenses against Bacterial Pore-Forming Toxin In Vivo. PLoS Pathog 4(10): e1000176. doi:10.1371/journal.ppat.1000176

Editor: Frederick M. Ausubel, Massachusetts General Hospital, United States of America

Received: June 17, 2008; Accepted: September 15, 2008; Published: October 10, 2008

Copyright: © 2008 Bischof et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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