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The metabolic enzyme fructose-1,6-bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella

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  • Jason Ziveri

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 11: Pathogenesis of Systemic Infections)

  • Fabiola Tros

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 11: Pathogenesis of Systemic Infections)

  • Ida Chiara Guerrera

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM US24/CNRS UMS3633)

  • Cerina Chhuon

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM US24/CNRS UMS3633)

  • Mathilde Audry

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 11: Pathogenesis of Systemic Infections)

  • Marion Dupuis

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 11: Pathogenesis of Systemic Infections)

  • Monique Barel

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 11: Pathogenesis of Systemic Infections)

  • Sarantis Korniotis

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 16: Immunity in Health and Disease)

  • Simon Fillatreau

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 16: Immunity in Health and Disease)

  • Lara Gales

    (Université de Toulouse, CNRS, INRA, INSA)

  • Edern Cahoreau

    (Université de Toulouse, CNRS, INRA, INSA)

  • Alain Charbit

    (Université Paris Descartes, Sorbonne Paris Cité
    INSERM U1151 - CNRS UMR 8253, Institut Necker-Enfants Malades, Team 11: Pathogenesis of Systemic Infections)

Abstract

The enzyme fructose-bisphosphate aldolase occupies a central position in glycolysis and gluconeogenesis pathways. Beyond its housekeeping role in metabolism, fructose-bisphosphate aldolase has been involved in additional functions and is considered as a potential target for drug development against pathogenic bacteria. Here, we address the role of fructose-bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, we unravel a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively. We propose a model in which fructose-bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response.

Suggested Citation

  • Jason Ziveri & Fabiola Tros & Ida Chiara Guerrera & Cerina Chhuon & Mathilde Audry & Marion Dupuis & Monique Barel & Sarantis Korniotis & Simon Fillatreau & Lara Gales & Edern Cahoreau & Alain Charbit, 2017. "The metabolic enzyme fructose-1,6-bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella," Nature Communications, Nature, vol. 8(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00889-7
    DOI: 10.1038/s41467-017-00889-7
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