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dc.contributor.authorBeddoe, T.en
dc.contributor.authorPaton, A.en
dc.contributor.authorLe Nours, J.en
dc.contributor.authorRossjohn, J.en
dc.contributor.authorPaton, J.en
dc.identifier.citationTrends in Biochemical Sciences, 2010; 35(7):411-418en
dc.description.abstractAB5 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 diseasesen
dc.description.statementofresponsibilityTravis Beddoe, Adrienne W. Paton, Jérôme Le Nours, Jamie Rossjohn and James C. Patonen
dc.publisherElsevier Science Londonen
dc.rightsCopyright © 2010 Elsevier Ltd All rights reserveden
dc.subjectHumans; Polysaccharides; Bacterial Toxins; Molecular Structureen
dc.titleStructure, biological functions and applications of the AB5 toxinsen
dc.typeJournal articleen
pubs.library.collectionMolecular and Biomedical Science publicationsen
dc.identifier.orcidPaton, J. [0000-0001-9807-5278]en
Appears in Collections:Molecular and Biomedical Science publications

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