The increasing role of phosphatidylethanolamine as a lipid receptor in the action of host defence peptides

Phoenix, David A., Harris, Frederick, Mura, Manuela and Dennison, Sarah R. (2015) The increasing role of phosphatidylethanolamine as a lipid receptor in the action of host defence peptides. Progress in Lipid Research, 59 . pp. 26-37. ISSN 0163-7827

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The increasing role of phosphatidylethanolamine as a lipid receptor in the action of host defence peptides

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Abstract

Host defence peptides (HDPs) are antimicrobial agents produced by organisms across the prokaryotic and eukaryotic kingdoms. Many prokaryotes produce HDPs, which utilise lipid and protein receptors in the membranes of bacterial competitors to facilitate their antibacterial action and thereby survive in their niche environment. As a major example, it is well established that cinnamycin and duramycins from Streptomyces have a high affinity for phosphatidylethanolamine (PE) and exhibit activity against other Gram-positive organisms, such as Bacillus. In contrast, although eukaryotic HDPs utilise membrane interactive mechanisms to facilitate their antimicrobial activity, the prevailing view has long been that these mechanisms do not involve membrane receptors. However, this view has been recently challenged by reports that a number of eukaryotic HDPs such as plant cyclotides also use PE as a receptor to promote their antimicrobial activities. Here, we review current understanding of the mechanisms that underpin the use of PE as a receptor in the antimicrobial and other biological actions of HDPs and describe medical and biotechnical uses of these peptides, which range from tumour imaging and detection to inclusion in topical microbicidal gels to prevent the sexual transmission of HIV. © 2015 Elsevier Ltd. All rights reserved.

Keywords:amyloid beta protein1-40, amyloid beta protein1-42, amyloid forming host defence peptide, antiinfective agent, cyclotide, cycloviolacin O2, host defence peptide, kalata B1, kalata B2, lancovutide, lanthiopeptin, lantibiotic, maximin H5, phosphatidylethanolamine, unclassified drug, antimicrobial activity, Bacillus, binding affinity, biological activity, drug binding site, drug receptor binding, drug synthesis, Gram positive bacterium, human, lipid analysis, membrane binding, nonhuman, peptide analysis, priority journal, Review, Streptomyces, structure activity relation, Bacillus (bacterium), Bacteria (microorganisms), Eukaryota, Posibacteria, Prokaryota, JCNotOpen
Subjects:C Biological Sciences > C500 Microbiology
Divisions:College of Science > School of Mathematics and Physics
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ID Code:17750
Deposited On:15 Jul 2015 15:24

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