ArticlePLoS pathogens2014
Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- A Single Amino Acid in the A2 Linker of Cholera Toxin Affects the Efficiency of Toxin Disassembly and Resulting Toxicity.ACS omega · 2026Article
- Protein disulfide isomerase dissolves and detoxifies oligomeric assemblies of amyloid beta peptide.FEBS letters · 2026Article
- Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique.In silico pharmacology · 2024Article
- Reduction is sufficient for the disassembly of ricin and Shiga toxin 1 but notInfection and immunity · 2023Article
- The cytopathic activity of cholera toxin requires a threshold quantity of cytosolic toxin.Cellular signalling · 2023Article
- Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin.Scientific reports · 2022Article
- Requirement of Peptidyl-Prolyl Cis/Trans isomerases and chaperones for cellular uptake of bacterial AB-type toxins.Frontiers in cellular and infection microbiology · 2022Review
- cAMP-Independent Activation of the Unfolded Protein Response by Cholera Toxin.Infection and immunity · 2021Article
- Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase.Frontiers in cell and developmental biology · 2020Article
- Male-Specific Protein Disulphide Isomerase Function is Essential for Plasmodium Transmission and a Vulnerable Target for Intervention.Scientific reports · 2019Article
- Stability and Conformational Resilience of Protein Disulfide Isomerase.Biochemistry · 2019Article
- HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.The Journal of biological chemistry · 2019Article
- Quercetin-3-Rutinoside Blocks the Disassembly of Cholera Toxin by Protein Disulfide Isomerase.Toxins · 2019Article
- Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process.International journal of molecular sciences · 2019Review
- Protein disulfide isomerase does not act as an unfoldase in the disassembly of cholera toxin.Bioscience reports · 2018Article
- Cell Propagation of Cholera Toxin CTA ADP-Ribosylating Factor by Exosome Mediated Transfer.International journal of molecular sciences · 2018Article
- Article
- A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin.Toxins · 2015Article
- Analysis of the isomerase and chaperone-like activities of an amebic PDI (EhPDI).BioMed research international · 2015Article
- A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease.Critical reviews in biochemistry and molecular biology · 2015Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
To generate a cytopathic effect, the catalytic A1 subunit of cholera toxin (CT) must be separated from the rest of the toxin. Protein disulfide isomerase (PDI) is thought to mediate CT disassembly by acting as a redox-driven chaperone that actively unfolds the CTA1 subunit. Here, we show that PDI itself unfolds upon contact with CTA1. The substrate-induced unfolding of PDI provides a novel molecular mechanism for holotoxin disassembly: we postulate the expanded hydrodynamic radius of unfolded PDI acts as a wedge to dislodge reduced CTA1 from its holotoxin. The oxidoreductase activity of PDI was not required for CT disassembly, but CTA1 displacement did not occur when PDI was locked in a folded conformation or when its substrate-induced unfolding was blocked due to the loss of chaperone function. Two other oxidoreductases (ERp57 and ERp72) did not unfold in the presence of CTA1 and did not displace reduced CTA1 from its holotoxin. Our data establish a new functional property of PDI that may be linked to its role as a chaperone that prevents protein aggregation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.