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Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence.
Hicks, Kevin G; Delbecq, Scott P; Sancho-Vaello, Enea; Blanc, Marie-Pierre; Dove, Katja K; Prost, Lynne R; Daley, Margaret E; Zeth, Kornelius; Klevit, Rachel E; Miller, Samuel I.
Afiliación
  • Hicks KG; Department of Microbiology, University of Washington Medical School, Seattle, United States.
  • Delbecq SP; Department of Biochemistry, University of Washington Medical School, Seattle, United States.
  • Sancho-Vaello E; Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain.
  • Blanc MP; Department of Microbiology, University of Washington Medical School, Seattle, United States.
  • Dove KK; Department of Biochemistry, University of Washington Medical School, Seattle, United States.
  • Prost LR; Department of Biochemistry, University of Wisconsin-Madison, Madison, United States.
  • Daley ME; Department of Chemistry and Biochemistry, University of San Diego, San Diego, United States.
  • Zeth K; Department of Biochemistry and Molecular Biology, University of Basque Country, Leioa, Spain.
  • Klevit RE; Department of Biochemistry, University of Washington Medical School, Seattle, United States.
  • Miller SI; Department of Microbiology, University of Washington Medical School, Seattle, United States.
Elife ; 4: e06792, 2015 May 23.
Article en En | MEDLINE | ID: mdl-26002083
Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is repressed by divalent cations and induced in environments of acidic pH, limited divalent cations, and cationic antimicrobial peptides (CAMP). Previously, it was unclear which signals are sensed by salmonellae to promote PhoQ-mediated virulence. We defined conformational changes produced in the PhoQ PD on exposure to acidic pH that indicate structural flexibility is induced in α-helices 4 and 5, suggesting this region contributes to pH sensing. Therefore, we engineered a disulfide bond between W104C and A128C in the PhoQ PD that restrains conformational flexibility in α-helices 4 and 5. PhoQ(W104C-A128C) is responsive to CAMP, but is inhibited for activation by acidic pH and divalent cation limitation. phoQ(W104C-A128C) Salmonella enterica Typhimurium is virulent in mice, indicating that acidic pH and divalent cation sensing by PhoQ are dispensable for virulence.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Salmonella typhimurium / Proteínas Bacterianas / Cationes Bivalentes / Regulación Bacteriana de la Expresión Génica / Factores de Virulencia / Concentración de Iones de Hidrógeno Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Elife Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Salmonella typhimurium / Proteínas Bacterianas / Cationes Bivalentes / Regulación Bacteriana de la Expresión Génica / Factores de Virulencia / Concentración de Iones de Hidrógeno Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Elife Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido