title: Fighting microbial infections: A lesson from amphibian skin-derived esculentin-1 peptides.
abstract: Due to the growing emergence of resistance to commercially available antibiotics/antimycotics in virtually all clinical microbial pathogens, the discovery of alternative anti-infective agents, is greatly needed. Gene-encoded antimicrobial peptides (AMPs) hold promise as novel therapeutics. In particular, amphibian skin is one of the richest storehouses of AMPs, especially that of the genus Rana, with esculentins-1 being among the longest (46 amino acids) AMPs found in nature to date. Here, we report on the recently discovered in vitro and in vivo activities and mechanism of action of two derivatives of the N-terminal part of esculentin-1a and -1b peptides, primarily against two relevant opportunistic microorganisms causing a large number of life-threatening infections worldwide; i.e. the Gram-negative bacterium Pseudomonas aeruginosa and the yeast Candida albicans. Because of distinct advantages compared to several mammalian AMPs, the two selected frog skin AMP-derivatives represent attractive candidates for the development of new antimicrobial compounds with expanded properties, for both human and veterinary medicine.
authors.affiliation: Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Piazzale Aldo Moro, 5-00185 Rome, Italy. Electronic address: marialuisa.mangoni@uniroma1.it.
authors.forename: Maria Luisa
authors.initials: ML
authors.lastname: Mangoni
authors.affiliation: Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Piazzale Aldo Moro, 5-00185 Rome, Italy.
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Luca
authors.affiliation: The Ocular Surface Institute, College of Optometry, University of Houston, Houston, TX, USA.
authors.forename: Alison M
authors.initials: AM
authors.lastname: McDermott
mesh_terms: D029845:Amphibian Proteins / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D002175:Candida / Q000254:growth & development*; D002177:Candidiasis / Q000188:drug therapy*; D006801:Humans; D011552:Pseudomonas Infections / Q000188:drug therapy*; D011550:Pseudomonas aeruginosa / Q000254:growth & development*; D011898:Ranidae; D012867:Skin / Q000737:chemistry*
chemical_list: D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; C092874:esculentin protein, Rana esculenta
keywords: Antimicrobial peptide; Cystic fibrosis; Frog skin; Infectious diseases; Innate immunity; Keratitis