title: The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives.
abstract: Members of the RTX family of protein toxins are functionally conserved among an assortment of bacterial pathogens. By disrupting host cell integrity through their pore-forming and cytolytic activities, this class of toxins allows pathogens to effectively tamper with normal host cell processes, promoting pathogenesis. Here, we focus on the biology of RTX toxins by describing salient properties of a prototype member, α-hemolysin, which is often encoded by strains of uropathogenic Escherichia coli. It has long been appreciated that RTX toxins can have distinct effects on host cells aside from outright lysis. Recently, advances in modeling and analysis of host-pathogen interactions have led to novel findings concerning the consequences of pore formation during host-pathogen interactions. We discuss current progress on longstanding questions concerning cell specificity and pore formation, new areas of investigation that involve toxin-mediated perturbations of host cell signaling cascades and perspectives on the future of RTX toxin investigation.
authors.affiliation: Division of Microbiology & Immunology, Pathology Department, University of Utah, 15 North Medical Drive East #2100, Salt Lake City, UT 84112-0565, USA.
authors.forename: Travis J
authors.initials: TJ
authors.lastname: Wiles
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Mulvey
mesh_terms: D000818:Animals; D001427:Bacterial Toxins / Q000235:genetics / Q000378:metabolism*; D006460:Hemolysin Proteins / Q000235:genetics / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D006801:Humans; D056689:Uropathogenic Escherichia coli / Q000235:genetics / Q000378:metabolism*
chemical_list: D001427:Bacterial Toxins; D006460:Hemolysin Proteins