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

Open access
Breukink, E., Wiedemann, I., Kraaij, C. van, Kuipers, O. P., Sahl, H.-G., de Kruijff, B.·1999·Science

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).

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Metadata

Authors
Breukink, E., Wiedemann, I., Kraaij, C. V., Kuipers, O. P., Sahl, H.-G., & de Kruijff, B.
Venue
Science
Published
1999-12-17
Volume
286
Issue
5448
Pages
2361-2364
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1968125869
Cited by
814
References
0
FWCI
18.34
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic. https://app.cochat.ai/papers/10.1126/science.286.5448.2361
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Breukink, E., Wiedemann, I., Kraaij, C. V., Kuipers, O. P., Sahl, H.-G., & de Kruijff, B. (1999). Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic. Science. https://doi.org/10.1126/science.286.5448.2361

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.