A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin

A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin

Cholera toxin (CT) consists of a catalytic A1 subunit, an A2 linker, and a homopentameric cell-binding B subunit. The intact holotoxin moves by vesicle carriers from the cell surface to the endoplasmic reticulum (ER) where CTA1 is released from the rest of the toxin. The dissociated CTA1 subunit t...

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Bibliographic Details
Main Authors: Michael Taylor, David Curtis, Ken Teter
Format: Article
Language:English
Published: MDPI AG 2015-07-01
Series:Toxins
Subjects:
cholera toxin
endoplasmic reticulum
protein disulfide isomerase
surface plasmon resonance
toxin assembly
toxin instability
Online Access:http://www.mdpi.com/2072-6651/7/7/2674

Internet

http://www.mdpi.com/2072-6651/7/7/2674

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