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  • 1
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    Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: 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).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breukink, E -- Wiedemann, I -- van Kraaij, C -- Kuipers, O P -- Sahl, H G -- de Kruijff, B -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center of Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, Institute for Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600751" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/metabolism/*pharmacology ; Cell Membrane/drug effects/metabolism ; Cell Membrane Permeability/drug effects ; Cell Wall/metabolism ; Dose-Response Relationship, Drug ; Membrane Lipids/metabolism ; Microbial Sensitivity Tests ; Micrococcus/*drug effects/metabolism ; Molecular Sequence Data ; Nisin/*analogs & derivatives/metabolism/pharmacology ; Peptides/pharmacology ; Peptidoglycan ; Polyisoprenyl Phosphate Oligosaccharides/*metabolism ; Vancomycin/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-16
    Description: Lantibiotics are polycyclic peptides containing unusual amino acids, which have binding specificity for bacterial cells, targeting the bacterial cell wall component lipid II to form pores and thereby lyse the cells. Yet several members of these lipid II-targeted lantibiotics are too short to be able to span the lipid bilayer and cannot form pores, but somehow they maintain their antibacterial efficacy. We describe an alternative mechanism by which members of the lantibiotic family kill Gram-positive bacteria by removing lipid II from the cell division site (or septum) and thus block cell wall synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasper, Hester E -- Kramer, Naomi E -- Smith, James L -- Hillman, J D -- Zachariah, Cherian -- Kuipers, Oscar P -- de Kruijff, Ben -- Breukink, Eefjan -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1636-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry of Membranes, Bijvoet Center for Biomolecular Research, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH, Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973881" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/metabolism/*pharmacology ; Bacillus/*drug effects/metabolism/ultrastructure ; Bacillus megaterium/drug effects/metabolism/ultrastructure ; Bacillus subtilis/drug effects/metabolism/ultrastructure ; Bacteriocins/chemistry/*metabolism/*pharmacology ; Cell Division/drug effects ; Cell Wall/metabolism ; Lipid Bilayers/metabolism ; Membranes, Artificial ; Nisin/chemistry/metabolism/pharmacology ; Peptides/chemistry/metabolism/pharmacology ; Peptidoglycan/biosynthesis ; Uridine Diphosphate N-Acetylmuramic Acid/*analogs & derivatives/metabolism ; Vancomycin/metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
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