title: Activities of four frog skin-derived antimicrobial peptides (temporin-1DRa, temporin-1Va and the melittin-related peptides AR-23 and RV-23) against anaerobic bacteria.
abstract: The activities of two antimicrobial peptides belonging to the temporin family (temporin-1DRa from Rana draytonii and temporin-1Va from Rana virgatipes) and two peptides with structural similarity to the bee venom peptide melittin (AR-23 from Rana tagoi and RV-23 from R. draytonii) were evaluated against a range of reference strains and clinical isolates of anaerobic bacteria. These peptides were selected because they show broad-spectrum growth inhibitory activity against reference strains of several medically important aerobic microorganisms and against clinical isolates of methicillin-resistant Staphylococcus aureus. All peptides showed relatively high potency (minimum inhibitory concentration (MIC) </=25 microM) against the Gram-positive bacilli Propionibacterium acnes and Clostridium tertium and the Gram-positive cocci Peptostreptococcus anaerobius. Activity was lower and more variable against Clostridium septicum, Clostridium perfringens and Peptostreptococcus asaccharolyticus. Growth of the Gram-negative bacilli Bacteroides fragilis and Fusobacterium spp. was poorly inhibited, but all the peptides were active (MIC</=25 microM) against Prevotella melaninogenica. The clinical utility of the melittin-related peptides is limited by their toxicities, but temporin-1DRa and temporin-1Va have relatively low haemolytic activity against human erythrocytes and so represent candidates for drug development, particularly for topical therapy of infected surface lesions.
authors.affiliation: Department of Clinical Microbiology, Faculty of Medicine, University of Szeged, Szeged, Hungary.
authors.forename: Edit
authors.initials: E
authors.lastname: Urbán
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Nagy
authors.forename: Tibor
authors.initials: T
authors.lastname: Pál
authors.forename: Agnes
authors.initials: A
authors.lastname: Sonnevend
authors.forename: J Michael
authors.initials: JM
authors.lastname: Conlon
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D000900:Anti-Bacterial Agents / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology*; D001421:Bacteria, Anaerobic / Q000187:drug effects*; D008555:Melitten / Q000235:genetics / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D011898:Ranidae / Q000235:genetics / Q000378:metabolism*; D012867:Skin / Q000378:metabolism
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C475804:melittin-related peptide, Rana tagoi; C104501:temporin; D008555:Melitten