title: Adventures of a pore-forming toxin at the target cell surface.
abstract: The past three years have shed light on how the pore-forming toxin aerolysin binds to its target cell and then hijacks cellular devices to promote its own polymerization and pore formation. This selective permeabilization of the plasma membrane has unexpected intracellular consequences that might explain the importance of aerolysin in Aeromonas pathogenicity.
authors.affiliation: Dept of Biochemistry, University of Geneva, 30 quai E. Ansermet, 1211 Geneva 4, Switzerland.
authors.forename: L
authors.initials: L
authors.lastname: Abrami
authors.forename: M
authors.initials: M
authors.lastname: Fivaz
authors.forename: F G
authors.initials: FG
authors.lastname: van der Goot
mesh_terms: D016980:Aeromonas hydrophila / Q000378:metabolism / Q000472:pathogenicity*; D000818:Animals; D001427:Bacterial Toxins / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D001704:Biopolymers / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism* / Q000382:microbiology; D002463:Cell Membrane Permeability / Q000187:drug effects; D006801:Humans; D052899:Pore Forming Cytotoxic Proteins; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism
chemical_list: D001427:Bacterial Toxins; D001704:Biopolymers; D052899:Pore Forming Cytotoxic Proteins; D011956:Receptors, Cell Surface; C032676:aerolysin