Activities of four frog skin-derived antimicrobial peptides (temporin-1DRa, temporin-1Va abd metillin-related peptides AR-23 and RV-23) against anaerobic bacteria
Institute of Medical Microbiology and Immunology, University of Pécs, Fuenfkirchen, Baranya, Hungary International Journal of Antimicrobial Agents
(Impact Factor: 4.3).
04/2007; 29(3):317-21. DOI: 10.1016/j.ijantimicag.2006.09.007
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.
Available from: Dewen You
- "Several antimicrobial peptides including epinecidin- and granulysin-derived peptides, and frog skin peptides have been found to exert anti-P. acnes functions –. Recently, sebocytes are found to express functional cathelicidin antimicrobial peptides with activity to kill P. acnes . Considering anti-inflammatory activities of some antimicrobial peptides, they are suggested to be potent agents for acne vulgaris treatment . "
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ABSTRACT: Cathelicidins are a family of antimicrobial peptides acting as multifunctional effector molecules in innate immunity. Cathelicidin-BF has been purified from the snake venoms of Bungarus fasciatus and it is the first identified cathelicidin antimicrobial peptide in reptiles. In this study, cathelicidin-BF was found exerting strong antibacterial activities against Propionibacterium acnes. Its minimal inhibitory concentration against two strains of P. acnes was 4.7 µg/ml. Cathelicidin-BF also effectively killed other microorganisms including Staphylococcus epidermidis, which was possible pathogen for acne vulgaris. Cathelicidin-BF significantly inhibited pro-inflammatory factors secretion in human monocytic cells and P. acnes-induced O2.- production of human HaCaT keratinocyte cells. Observed by scanning electron microscopy, the surfaces of the treated pathogens underwent obvious morphological changes compared with the untreated controls, suggesting that this antimicrobial peptide exerts its action by disrupting membranes of microorganisms. The efficacy of cathelicidin-BF gel topical administering was evaluated in experimental mice skin colonization model. In vivo anti-inflammatory effects of cathelicidin-BF were confirmed by relieving P. acnes-induced mice ear swelling and granulomatous inflammation. The anti-inflammatory effects combined with potent antimicrobial activities and O2.- production inhibition activities of cathelicidin-BF indicate its potential as a novel therapeutic option for acne vulgaris.
Available from: Sabine Melzer
- "In vitro growth inhibition assays have been widely used to determine the effectiveness of skin secretions and isolated peptides against a range of different microorganisms (Rollins- Smith et al., 2002a; Urban et al., 2007; Mangoni et al., 2008; Sheafor et al., 2008). The skin secretions of Leiopelmatid species contain a variety of novel peptides and compounds with anti-chytrid properties, which are in the process of being identified (S. "
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ABSTRACT: Over the past few decades, amphibian populations have undergone drastic declines on a global scale. Declines in many anuran populations have been linked to the emergent skin-invasive amphibian chytrid fungus Batrachochytrium dendrobatidis (Bd). Antimicrobial peptides in the skin are thought to act as important components of the innate immune system that may protect some species from infectious diseases. The four archaic species of Leiopelma in New Zealand are of great conservation concern and a severe population crash of Leiopelma archeyi between 1996 and 2001 has been tentatively linked with the outbreak of Bd. Here, we investigated the in vitro activity of skin secretions of six frog species in New Zealand against Bd zoospore growth. The activity of skin secretions produced by frogs in the wild varied significantly between species, with those of Le. archeyi being the most active. The skin secretions of native Leiopelmatid species showed greater Bd zoospore inhibition (31.0–71.9%) than the naturalized Litoria species (17.4–18.2%). Leiopelma archeyi has the most active peptides, even though it is the only native species with known susceptibility to Bd infections.
Available from: onlinelibrary.wiley.com
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Dr Roberto Romero did not participate in the drafting of the text, nor did he review, approve or endorse this manuscript. This article is not approved or endorsed by Perinatology Research Branch, the National Institute of Child Health and Human Development (NICHD), the National Institutes of Health (NIH), or the Department of Health and Human Services of the USA.
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