Cholera toxin: A paradigm for multi-functional engagement of cellular mechanisms (Review)

@article{Haan2004CholeraTA,
  title={Cholera toxin: A paradigm for multi-functional engagement of cellular mechanisms (Review)},
  author={Lolke de Haan and Timothy Raymond Hirst},
  journal={Molecular Membrane Biology},
  year={2004},
  volume={21},
  pages={77 - 92}
}
Cholera toxin (Ctx) from Vibrio cholerae and its closely related homologue, heat-labile enterotoxin (Etx) from Escherichia coli have become superb tools for illuminating pathways of cellular trafficking and immune cell function. These bacterial protein toxins should be viewed as conglomerates of highly evolved, multi-functional elements equipped to engage the trafficking and signalling machineries of cells. Ctx and Etx are members of a larger family of A-B toxins of bacterial (and plant) origin… 
Vibrio cholerae: cholera toxin.
A Therapeutic Chemical Chaperone Inhibits Cholera Intoxication and Unfolding/Translocation of the Cholera Toxin A1 Subunit
TLDR
It is shown by circular dichroism and fluorescence spectroscopy that exposure to 4-phenylbutyric acid (PBA) inhibited the thermal unfolding of CTA1, which blocked the ER-to-cytosol export of Cta1 and productive intoxication of either cultured cells or rat ileal loops.
Grape Extracts Inhibit Multiple Events in the Cell Biology of Cholera Intoxication
TLDR
Two grape extracts currently sold as nutritional supplements inhibited CT and Escherichia coli heat-labile toxin activity against cultured cells and intestinal loops and disrupted the catalytic activity of CTA1.
Characterization of Fluorescent Chimeras of Cholera Toxin and Escherichia coli Heat-Labile Enterotoxins Produced by Use of the Twin Arginine Translocation System
TLDR
Fluorescent fusion proteins were shown to assemble spontaneously and efficiently with the corresponding B polypeptides in the periplasm to form chimeric holotoxin-like molecules, and these chimeras bound to and entered cultured cells in a manner similar to native CT, LTI, or LTIIb.
Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins.
Bacterial ADP-ribosylating toxins are the causative agents for several severe human and animal diseases such as diphtheria, cholera, or enteric diseases. They display an AB-type structure: The
Cholera Toxin Interactions with Host Cell Stress Proteins
TLDR
The intrinsic conformational instability of the CTA1 polypeptide drives host-toxin interactions related to the translocation event and involves both standard and atypical functions for a variety of host chaperones.
Modulation of Cholera Toxin Structure/Function by Hsp90
TLDR
Hsp90 plays two key roles CT intoxication: it couples toxin refolding with toxin extraction from the ER, and it maintains the cytosolic toxin in a functional conformation.
Brefeldin A and Exo1 Completely Releave the Block of Cholera Toxin Action by a Dipeptide Metalloendoprotease Substrate
Cholera toxin (CT), the enterotoxin secreted by Vibrio cholerae classical as well as El Tor biotypes, is the major causative agent of the acute diarrheal disease of humans. CT and the Escherichia
An outer membrane channel protein of Mycobacterium tuberculosis with exotoxin activity
TLDR
It is demonstrated that the M. tuberculosis protein Rv3903c (channel protein with necrosis-inducing toxin, CpnT), which forms a channel in the outer membrane and releases a toxic domain into the extracellular milieu, has a dual function in uptake of nutrients and induction of host cell death by M.culosis.
The Cholera Toxin A13 Subdomain Is Essential for Interaction with ADP-Ribosylation Factor 6 and Full Toxic Activity but Is Not Required for Translocation from the Endoplasmic Reticulum to the Cytosol
TLDR
It is found that the A13 subdomain of CTA1 is important both for interaction with ARF6 and for full expression of enzyme activity in vivo and Surprisingly, however, the A 13 subdomain was not required for ERAD-mediated passage of Cta1 from the ER to the cytosol.
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TLDR
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TLDR
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TLDR
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