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High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action

Author

Listed:
  • Francesca Zuttion

    (U1067 INSERM, Aix-Marseille Université)

  • Adai Colom

    (University of Geneva)

  • Stefan Matile

    (University of Geneva)

  • Denes Farago

    (Department of Technical Informatics University of Szeged)

  • Frédérique Pompeo

    (Laboratoire de Chimie Bactérienne (LCB), Institut de Microbiologie de la Méditerranée (IMM), CNRS, UMR 7283, Aix Marseille Université)

  • Janos Kokavecz

    (University of Szeged)

  • Anne Galinier

    (Laboratoire de Chimie Bactérienne (LCB), Institut de Microbiologie de la Méditerranée (IMM), CNRS, UMR 7283, Aix Marseille Université)

  • James Sturgis

    (LISM, UMR 7255, CNRS, Aix Marseille Université)

  • Ignacio Casuso

    (U1067 INSERM, Aix-Marseille Université)

Abstract

The increase in speed of the high-speed atomic force microscopy (HS-AFM) compared to that of the conventional AFM made possible the first-ever visualisation at the molecular-level of the activity of an antimicrobial peptide on a membrane. We investigated the medically prescribed but poorly understood lipopeptide Daptomycin under infection-like conditions (37 °C, bacterial lipid composition and antibiotic concentrations). We confirmed so far hypothetical models: Dap oligomerization and the existence of half pores. Moreover, we detected unknown molecular mechanisms: new mechanisms to form toroidal pores or to resist Dap action, and to unprecedently quantify the energy profile of interacting oligomers. Finally, the biological and medical relevance of the findings was ensured by a multi-scale multi-nativeness—from the molecule to the cell—correlation of molecular-level information from living bacteria (Bacillus subtilis strains) to liquid-suspended vesicles and supported-membranes using electron and optical microscopies and the lipid tension probe FliptR, where we found that the cells with a healthier state of their cell wall show smaller membrane deformations.

Suggested Citation

  • Francesca Zuttion & Adai Colom & Stefan Matile & Denes Farago & Frédérique Pompeo & Janos Kokavecz & Anne Galinier & James Sturgis & Ignacio Casuso, 2020. "High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19710-z
    DOI: 10.1038/s41467-020-19710-z
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    Cited by:

    1. Telmo O. Paiva & Albertus Viljoen & Yves F. Dufrêne, 2022. "Seeing the unseen: High-resolution AFM imaging captures antibiotic action in bacterial membranes," Nature Communications, Nature, vol. 13(1), pages 1-3, December.
    2. Adéla Melcrová & Sourav Maity & Josef Melcr & Niels A. W. Kok & Mariella Gabler & Jonne Eyden & Wenche Stensen & John S. M. Svendsen & Arnold J. M. Driessen & Siewert J. Marrink & Wouter H. Roos, 2023. "Lateral membrane organization as target of an antimicrobial peptidomimetic compound," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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