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Delivery of cardiolipins to the Salmonella outer membrane is necessary for survival within host tissues and virulence.
Dalebroux, Zachary D; Edrozo, Mauna B; Pfuetzner, Richard A; Ressl, Susanne; Kulasekara, Bridget R; Blanc, Marie-Pierre; Miller, Samuel I.
Affiliation
  • Dalebroux ZD; Department of Microbiology, University of Washington, Seattle, WA 98195, USA.
  • Edrozo MB; Department of Microbiology, University of Washington, Seattle, WA 98195, USA.
  • Pfuetzner RA; Department of Microbiology, University of Washington, Seattle, WA 98195, USA.
  • Ressl S; Department of Molecular and Cellular Biochemistry, Indiana University Bloomington, 212 S. Hawthrone Drive, Bloomington, IN 47401, USA.
  • Kulasekara BR; Department of Microbiology, University of Washington, Seattle, WA 98195, USA.
  • Blanc MP; Department of Microbiology, University of Washington, Seattle, WA 98195, USA.
  • Miller SI; Department of Microbiology, University of Washington, Seattle, WA 98195, USA; Department of Genome Sciences, University of Washington, Seattle, WA 98195, USA; Department of Medicine, University of Washington, Seattle, WA 98195, USA. Electronic address: millersi@uw.edu.
Cell Host Microbe ; 17(4): 441-51, 2015 Apr 08.
Article in En | MEDLINE | ID: mdl-25856753
ABSTRACT
The outer membrane (OM) of Gram-negative bacteria is an asymmetric lipid bilayer that serves as a barrier to the environment. During infection, Gram-negative bacteria remodel their OM to promote survival and replication within host tissues. Salmonella rely on the PhoPQ two-component regulators to coordinate OM remodeling in response to environmental cues. In a screen for mediators of PhoPQ-regulated OM remodeling in Salmonella Typhimurium, we identified PbgA, a periplasmic domain-containing transmembrane protein, which binds cardiolipin glycerophospholipids near the inner membrane and promotes their PhoPQ-regulated trafficking to the OM. Purified-PbgA oligomers are tetrameric, and the periplasmic domain contains a globular region that binds to the OM in a PhoPQ-dependent manner. Thus, PbgA forms a complex that may bridge the envelope for regulated cardiolipin delivery. PbgA globular region-deleted mutant bacteria are severely attenuated for pathogenesis, suggesting that increased cardiolipin trafficking to the OM is necessary for Salmonella to survive within host tissues that activate PhoPQ.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Salmonella typhimurium / Bacterial Proteins / Cardiolipins / Cell Membrane / Host-Pathogen Interactions / Membrane Proteins Language: En Journal: Cell Host Microbe Journal subject: MICROBIOLOGIA Year: 2015 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Salmonella typhimurium / Bacterial Proteins / Cardiolipins / Cell Membrane / Host-Pathogen Interactions / Membrane Proteins Language: En Journal: Cell Host Microbe Journal subject: MICROBIOLOGIA Year: 2015 Document type: Article Affiliation country: United States