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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.
Afiliación
  • 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 en En | MEDLINE | ID: mdl-25856753
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Salmonella typhimurium / Proteínas Bacterianas / Cardiolipinas / Membrana Celular / Interacciones Huésped-Patógeno / Proteínas de la Membrana Idioma: En Revista: Cell Host Microbe Asunto de la revista: MICROBIOLOGIA Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Salmonella typhimurium / Proteínas Bacterianas / Cardiolipinas / Membrana Celular / Interacciones Huésped-Patógeno / Proteínas de la Membrana Idioma: En Revista: Cell Host Microbe Asunto de la revista: MICROBIOLOGIA Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos