Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic

E Breukink*, [No Value] Wiedemann, C van Kraaij, OP Kuipers, HG Sahl, B de Kruijff, I. Wiedemann

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

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).

Original languageEnglish
Pages (from-to)2361-2364
Number of pages4
JournalScience
Volume286
Issue number5448
DOIs
Publication statusPublished - 17-Dec-1999

Keywords

  • C-TERMINAL PART
  • ANTIMICROBIAL PEPTIDE
  • BACTERIAL-MEMBRANES
  • NISIN
  • TRANSLOCATION
  • VANCOMYCIN
  • VESICLES
  • BILAYERS

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