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Science 17 December 1999:
Vol. 286. no. 5448, pp. 2361 - 2364
DOI: 10.1126/science.286.5448.2361
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Reports

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

E. Breukink, 1* I. Wiedemann, 2 C. van Kraaij, 3 O. P. Kuipers, 4 H.-G. Sahl, 2 B. de Kruijff 1

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).

1 Center of Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, Institute for Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.
2 Institute for Medical Microbiology and Immunology, University of Bonn, Sigmund-Freud-Strasse 25, D-53105 Bonn, Germany.
3 NIZO Food Research, Microbial Ingredients Section, Post Office Box 20, 6710 BA Ede, Netherlands.
4 Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Post Office Box 14, 9750 AA Haren, Netherlands.
*   To whom correspondence should be addressed. E-mail: e.j.breukink{at}chem.uu.nl

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