Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
Type: Journal article
Title: Structure, biological functions and applications of the AB5 toxins
Author: Beddoe, T.
Paton, A.
Le Nours, J.
Rossjohn, J.
Paton, J.
Citation: Trends in Biochemical Sciences, 2010; 35(7):411-418
Publisher: Elsevier Science London
Issue Date: 2010
ISSN: 0968-0004
Statement of
Travis Beddoe, Adrienne W. Paton, Jérôme Le Nours, Jamie Rossjohn and James C. Paton
Abstract: AB5 toxins are important virulence factors for several major bacterial pathogens, including Bordetella pertussis, Vibrio cholerae, Shigella dysenteriae and at least two distinct pathotypes of Escherichia coli. The AB5 toxins are so named because they comprise a catalytic A-subunit, which is responsible for disruption of essential host functions, and a pentameric B-subunit that binds to specific glycan receptors on the target cell surface. The molecular mechanisms by which the AB5 toxins cause disease have been largely unravelled, including recent insights into a novel AB5 toxin family, subtilase cytotoxin (SubAB). Furthermore, AB5 toxins have become a valuable tool for studying fundamental cellular functions, and are now being investigated for potential applications in the clinical treatment of human diseases
Keywords: Humans; Polysaccharides; Bacterial Toxins; Molecular Structure
Rights: Copyright © 2010 Elsevier Ltd All rights reserved
RMID: 0020095432
DOI: 10.1016/j.tibs.2010.02.003
Description (link):
Appears in Collections:Molecular and Biomedical Science publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.