Next Article in Journal
Effects of Antagonists on Mycotoxins of Seedborne Fusarium spp. in Sweet Corn
Next Article in Special Issue
Pertussis Toxin: A Key Component in Pertussis Vaccines?
Previous Article in Journal
Diversity, Cyanotoxin Production, and Bioactivities of Cyanobacteria Isolated from Freshwaters of Greece
Previous Article in Special Issue
Assays for Determining Pertussis Toxin Activity in Acellular Pertussis Vaccines
Review

Intracellular Trafficking and Translocation of Pertussis Toxin

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32816, USA
Received: 6 July 2019 / Accepted: 24 July 2019 / Published: 25 July 2019
(This article belongs to the Special Issue Pertussis Toxin)
Pertussis toxin (PT) is a multimeric complex of six proteins. The PTS1 subunit is an ADP-ribosyltransferase that inactivates the alpha subunit of heterotrimeric Gi/o proteins. The remaining PT subunits form a pentamer that positions PTS1 in and above the central cavity of the triangular structure. Adhesion of this pentamer to glycoprotein or glycolipid conjugates on the surface of a target cell leads to endocytosis of the PT holotoxin. Vesicle carriers then deliver the holotoxin to the endoplasmic reticulum (ER) where PTS1 dissociates from the rest of the toxin, unfolds, and exploits the ER-associated degradation pathway for export to the cytosol. Refolding of the cytosolic toxin allows it to regain an active conformation for the disruption of cAMP-dependent signaling events. This review will consider the intracellular trafficking of PT and the order-disorder-order transitions of PTS1 that are essential for its cellular activity. View Full-Text
Keywords: AB toxin; chaperone; endocytosis; endoplasmic reticulum; ERAD; retrograde transport; translocation AB toxin; chaperone; endocytosis; endoplasmic reticulum; ERAD; retrograde transport; translocation
Show Figures

Figure 1

MDPI and ACS Style

Teter, K. Intracellular Trafficking and Translocation of Pertussis Toxin. Toxins 2019, 11, 437. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins11080437

AMA Style

Teter K. Intracellular Trafficking and Translocation of Pertussis Toxin. Toxins. 2019; 11(8):437. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins11080437

Chicago/Turabian Style

Teter, Ken. 2019. "Intracellular Trafficking and Translocation of Pertussis Toxin" Toxins 11, no. 8: 437. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins11080437

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop