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Changing the phospholipid composition of Staphylococcus aureus causes distinct changes in membrane proteome and membrane-sensory regulators

Authors

  • Susanne Sievers,

    Corresponding author
    1. Institute for Microbiology, Department of Microbial Physiology, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany
    • Institute for Microbiology, Department of Microbial Physiology, Ernst-Moritz-Arndt-University Greifswald, F.-L.-Jahn-Street 15, 17489 Greifswald, Germany Fax: +49-3834-86-42-02
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  • Christoph M. Ernst,

    1. Cellular and Molecular Microbiology Division, Interfacultary Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany
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  • Tobias Geiger,

    1. Interfacultary Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany
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  • Michael Hecker,

    1. Institute for Microbiology, Department of Microbial Physiology, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany
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  • Christiane Wolz,

    1. Interfacultary Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany
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  • Dörte Becher,

    1. Institute for Microbiology, Department of Microbial Physiology, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany
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  • Andreas Peschel

    1. Cellular and Molecular Microbiology Division, Interfacultary Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany
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Abstract

The dynamic lipid composition of bacterial cytoplasmic membranes has a profound impact on vital bacterial fitness and susceptibility to membrane-damaging agents, temperature, or osmotic stress. However, it has remained largely unknown how changes in lipid patterns affect the abundance and expression of membrane proteins. Using recently developed gel-free proteomics technology, we explored the membrane proteome of the important human pathogen Staphylococcus aureus in the presence or absence of the cationic phospholipid lysyl-phosphatidylglycerol (Lys-PG). We were able to detect almost half of all theoretical integral membrane proteins and could reliably quantify more than 35% of them. It is worth noting that the deletion of the Lys-PG synthase MprF did not lead to a massive alteration but a very distinct up- or down-regulation of only 1.5 or 3.5% of the quantified proteins. Lys-PG deficiency had no major impact on the abundance of lipid-biosynthetic enzymes but significantly affected the amounts of the cell envelope stress-sensing regulatory proteins such as SaeS and MsrR, and of the SaeS-regulated proteins Sbi, Efb, and SaeP. These data indicate very critical interactions of membrane-sensory proteins with phospholipids and they demonstrate the power of membrane proteomics for the characterization of bacterial physiology and pathogenicity.

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