title: Intoxication strategy of Helicobacter pylori VacA toxin.
abstract: VacA toxin from the cancer-inducing bacterium Helicobacter pylori is currently classified as a pore-forming toxin but is also considered a multifunctional toxin, apparently causing many pleiotropic cell effects. However, an increasing body of evidence suggests that VacA could be the prototype of a new class of monofunctional A-B toxins in which the A subunit exhibits pore-forming instead of enzymatic activity. Thus, VacA may use a peculiar mechanism of action, allowing it to intoxicate the human stomach. By combining the action of a cell-binding domain, a specific intracellular trafficking pathway and a novel mitochondrion-targeting sequence, the VacA pore-forming domain is selectively delivered to the inner mitochondrial membrane to efficiently kill target epithelial cells by apoptosis.
authors.affiliation: Department of Clinical Bacteriology, Nice University Hospital, 151 Route de Saint Antoine de Ginestière, 06202 Nice Cedex 03, France. Patrice.Boquet@unice.fr
authors.forename: Patrice
authors.initials: P
authors.lastname: Boquet
authors.forename: Vittorio
authors.initials: V
authors.lastname: Ricci
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism / Q000633:toxicity*; D016923:Cell Death; D004847:Epithelial Cells / Q000382:microbiology*; D016480:Helicobacter pylori / Q000472:pathogenicity*; D006801:Humans; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism; D051336:Mitochondrial Membranes / Q000187:drug effects / Q000502:physiology; D011485:Protein Binding; D021381:Protein Transport
chemical_list: D001426:Bacterial Proteins; C074689:VacA protein, Helicobacter pylori