Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.
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 it...
Main Authors: | Michael Taylor, Helen Burress, Tuhina Banerjee, Supriyo Ray, David Curtis, Suren A Tatulian, Ken Teter |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-02-01
|
Series: | PLoS Pathogens |
Online Access: | http://europepmc.org/articles/PMC3916401?pdf=render |
Similar Items
-
Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin
by: Albert Serrano, et al.
Published: (2022-01-01) -
Quercetin-3-Rutinoside Blocks the Disassembly of Cholera Toxin by Protein Disulfide Isomerase
by: Jessica Guyette, et al.
Published: (2019-08-01) -
A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin
by: Michael Taylor, et al.
Published: (2015-07-01) -
A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit.
by: Michael Taylor, et al.
Published: (2011-04-01) -
Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase
by: Albert Serrano, et al.
Published: (2020-07-01)