Protein disulfide isomerase a multifunctional protein with multiple physiological roles

H Ali Khan, B Mutus - Frontiers in chemistry, 2014 - frontiersin.org
Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox
proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide …

Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum

AIS Moretti, FRM Laurindo - Archives of biochemistry and biophysics, 2017 - Elsevier
Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin
superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in …

Requirement of Peptidyl-Prolyl Cis/Trans isomerases and chaperones for cellular uptake of bacterial AB-type toxins

K Ernst - Frontiers in Cellular and Infection Microbiology, 2022 - frontiersin.org
Bacterial AB-type toxins are proteins released by the producing bacteria and are the
causative agents for several severe diseases including cholera, whooping cough, diphtheria …

Toxins utilize the endoplasmic reticulum-associated protein degradation pathway in their intoxication process

J Nowakowska-Gołacka, H Sominka… - International Journal of …, 2019 - mdpi.com
Several bacterial and plant AB-toxins are delivered by retrograde vesicular transport to the
endoplasmic reticulum (ER), where the enzymatically active A subunit is disassembled from …

Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins

K Ernst, L Schnell, H Barth - Uptake and Trafficking of Protein Toxins, 2017 - Springer
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 …

Inhibition of cholera toxin and other AB toxins by polyphenolic compounds

P Cherubin, MC Garcia, D Curtis, CBT Britt, JW Craft Jr… - PloS one, 2016 - journals.plos.org
Cholera toxin (CT) is an AB-type protein toxin that contains a catalytic A1 subunit, an A2
linker, and a cell-binding B homopentamer. The CT holotoxin is released into the …

Reduction is sufficient for the disassembly of ricin and Shiga toxin 1 but not Escherichia coli heat-labile enterotoxin

JL Guyette, A Serrano, GR Huhn III, M Taylor… - Infection and …, 2023 - Am Soc Microbiol
Many AB toxins contain an enzymatic A moiety that is anchored to a cell-binding B moiety by
a disulfide bridge. After receptor-mediated endocytosis, some AB toxins undergo retrograde …

Co-and post-translocation roles for HSP90 in cholera intoxication

H Burress, M Taylor, T Banerjee, SA Tatulian… - Journal of Biological …, 2014 - ASBMB
Cholera toxin (CT) moves from the cell surface to the endoplasmic reticulum (ER) where the
catalytic CTA1 subunit separates from the rest of the toxin. CTA1 then unfolds and passes …

The manipulation of cell signaling and host cell biology by cholera toxin

C White, C Bader, K Teter - Cellular signalling, 2022 - Elsevier
Vibrio cholerae colonizes the small intestine and releases cholera toxin into the extracellular
space. The toxin binds to the apical surface of the epithelium, is internalized into the host …

HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol

H Burress, A Kellner, J Guyette, SA Tatulian… - Journal of Biological …, 2019 - ASBMB
Cholera toxin (CT) travels by vesicle carriers from the cell surface to the endoplasmic
reticulum (ER) where the catalytic A1 subunit of CT (CTA1) dissociates from the rest of the …