title: The pore-forming bacterial effector, VopQ, halts autophagic turnover.
abstract: Vibrio parahemolyticus Type III effector VopQ is both necessary and sufficient to induce autophagy within one hour of infection. We demonstrated that VopQ interacts with the Vo domain of the conserved vacuolar H(+)-ATPase. Membrane-associated VopQ subsequently forms pores in the membranes of acidic compartments, resulting in immediate release of protons without concomitant release of lumenal protein contents. These studies show how a bacterial pathogen can compromise host ion potentials using a gated pore-forming effector to equilibrate levels of small molecules found in endolysosomal compartments and disrupt cellular processes such as autophagy.
authors.affiliation: Department of Molecular Biology; UT Southwestern Medical Center; Dallas, TX USA.
authors.forename: Anju
authors.initials: A
authors.lastname: Sreelatha
authors.forename: Kim
authors.initials: K
authors.lastname: Orth
authors.forename: Vincent J
authors.initials: VJ
authors.lastname: Starai
mesh_terms: D001343:Autophagy; D001426:Bacterial Proteins / Q000378:metabolism* / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D052899:Pore Forming Cytotoxic Proteins / Q000378:metabolism* / Q000494:pharmacology; D014736:Vibrio parahaemolyticus / Q000378:metabolism / Q000472:pathogenicity*; D037521:Virulence Factors / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D001426:Bacterial Proteins; D052899:Pore Forming Cytotoxic Proteins; D037521:Virulence Factors
keywords: T3SS; Vibrio; VopQ; autophagy; channel; pore; virulence factor