Structure, biological functions and applications of the AB5 toxins

Travis Clarke Beddoe, Adrienne Webster Paton, Jerome Le Nours, Jamie Rossjohn, James C Paton

Research output: Contribution to journalArticleResearchpeer-review

207 Citations (Scopus)

Abstract

AB(5) 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 AB(5) 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 AB(5) toxins cause disease have been largely unravelled, including recent insights into a novel AB(5) toxin family, subtilase cytotoxin (SubAB). Furthermore, AB(5) 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.
Original languageEnglish
Pages (from-to)411 - 418
Number of pages8
JournalTrends in Biochemical Sciences
Volume35
Issue number7
DOIs
Publication statusPublished - 2010

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