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    Contribution of the Cpx envelope stress system to metabolism and virulence regulation in Salmonella enterica serovar Typhimurium (2019)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Subramaniam, Sivaraman
    Müller, Volker S.
    Hering, Nina A.
    Mollenkopf, Hans
    Becker, Daniel
    Heroven, Ann Kathrin
    Dersch, Petra
    Pohlmann, Anne
    Tedin, Karsten (WE 7)
    Porwollik, Steffen
    McClelland, Michael
    Meyer, Thomas F.
    Hunke, Sabine
    Quelle
    PLOS ONE
    Bandzählung: 14
    Heftzählung: 2
    Seiten: e0213297
    ISSN: 1932-6203
    Sprache
    Englisch
    Verweise
    URL (Volltext): https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0211584
    DOI: 10.1371/journal.pone.0211584
    Pubmed: 30716090
    Kontakt
    Institut für Mikrobiologie und Tierseuchen

    Robert-von-Ostertag-Str. 7-13
    14163 Berlin
    +49 30 838 51843 / 66949
    mikrobiologie@vetmed.fu-berlin.de

    Abstract / Zusammenfassung

    The Cpx-envelope stress system regulates the expression of virulence factors in many Gram-negative pathogens. In Salmonella enterica serovar Typhimurium deletion of the sensor kinase CpxA but not of the response regulator CpxR results in the down regulation of the key regulator for invasion, HilA encoded by the Salmonella pathogenicity island 1 (SPI-1). Here, we provide evidence that cpxA deletion interferes with dephosphorylation of CpxR resulting in increased levels of active CpxR and consequently in misregulation of target genes. 14 potential operons were identified to be under direct control of CpxR. These include the virulence determinants ecotin, the omptin PgtE, and the SPI-2 regulator SsrB. The Tat-system and the PocR regulator that together promote anaerobic respiration of tetrathionate on 1,2-propanediol are also under direct CpxR control. Notably, 1,2-propanediol represses hilA expression. Thus, our work demonstrates for the first time the involvement of the Cpx system in a complex network mediating metabolism and virulence function.