Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic

DOI Web Site 被引用文献24件
  • E. Breukink
    Center of Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, Institute for Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.
  • I. Wiedemann
    Institute for Medical Microbiology and Immunology, University of Bonn, Sigmund-Freud-Strasse 25, D-53105 Bonn, Germany.
  • C. van Kraaij
    NIZO Food Research, Microbial Ingredients Section, Post Office Box 20, 6710 BA Ede, Netherlands.
  • O. P. Kuipers
    Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Post Office Box 14, 9750 AA Haren, Netherlands.
  • H.-G. Sahl
    Institute for Medical Microbiology and Immunology, University of Bonn, Sigmund-Freud-Strasse 25, D-53105 Bonn, Germany.
  • B. de Kruijff
    Center of Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, Institute for Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.

抄録

<jats:p>Resistance to antibiotics is increasing in some groups of clinically important pathogens. For instance, high vancomycin resistance has emerged in enterococci. Promising alternative antibiotics are the peptide antibiotics, abundant in host defense systems, which kill their targets by permeabilizing the plasma membrane. These peptides generally do not act via specific receptors and are active in the micromolar range. Here it is shown that vancomycin and the antibacterial peptide nisin Z use the same target: the membrane-anchored cell wall precursor Lipid II. Nisin combines high affinity for Lipid II with its pore-forming ability, thus causing the peptide to be highly active (in the nanomolar range).</jats:p>

収録刊行物

  • Science

    Science 286 (5448), 2361-2364, 1999-12-17

    American Association for the Advancement of Science (AAAS)

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