Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin

Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin

Abstract Cholera toxin (CT) and Escherichia coli heat-labile enterotoxin (LT) are structurally similar AB5-type protein toxins. They move from the cell surface to the endoplasmic reticulum where the A1 catalytic subunit is separated from its holotoxin by protein disulfide isomerase (PDI), thus allow...

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Bibliographic Details
Main Authors: Albert Serrano, Jessica L. Guyette, Joel B. Heim, Michael Taylor, Patrick Cherubin, Ute Krengel, Ken Teter, Suren A. Tatulian
Format: Article
Language:English
Published: Nature Portfolio 2022-01-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-021-03939-9

Internet

https://doi.org/10.1038/s41598-021-03939-9

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