Structure, biological functions and applications of the AB5 toxins.
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.
Beddoe
Travis
T
The Protein Crystallography Unit, ARC Centre of Excellence in Structural and Functional Microbial Genomics, Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.
Paton
Adrienne W
AW
Le Nours
Jérôme
J
Rossjohn
Jamie
J
Paton
James C
JC
D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism* / Q000627:therapeutic use; D006801:Humans; D015394:Molecular Structure; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism
D001427:Bacterial Toxins; D011134:Polysaccharides