The increasing role of phosphatidylethanolamine as a lipid receptor in the action of host defence peptides.
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.
School of Applied Science, London South Bank University, 103 Borough Road, London SE1 0AA, UK. Electronic address: phoenixd@lsbu.ac.uk.
David A
DA
Phoenix
School of Applied Science, London South Bank University, 103 Borough Road, London SE1 0AA, UK; School of Forensic and Investigative Science, University of Central Lancashire, Preston PR1 2HE, UK.
Frederick
F
Harris
School of Mathematics and Physics, College of Science, University of Lincoln, Brayford Pool, Lincoln, Lincolnshire LN6 7TS, UK.
Manuela
M
Mura
School of Applied Science, London South Bank University, 103 Borough Road, London SE1 0AA, UK; School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston PR1 2HE, UK.
Sarah R
SR
Dennison
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D007113:Immunity, Innate; D008051:Lipid Bilayers / Q000737:chemistry; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010714:Phosphatidylethanolamines / Q000737:chemistry / Q000502:physiology*; D011485:Protein Binding
D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D010714:Phosphatidylethanolamines; C483858:phosphatidylethanolamine
Amyloid-forming host defence peptides; Cyclotides; Host defence peptides; Lantibiotics; Lipid receptors; Maximin H5; PE-binding; Phosphatidylethanolamine (PE)