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      Conventional and Unconventional Antimicrobials from Fish, Marine Invertebrates and Micro-algae

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          Abstract

          All eukaryotic organisms, single-celled or multi-cellular, produce a diverse array of natural anti-infective agents that, in addition to conventional antimicrobial peptides, also include proteins and other molecules often not regarded as part of the innate defences. Examples range from histones, fatty acids, and other structural components of cells to pigments and regulatory proteins. These probably represent very ancient defence factors that have been re-used in new ways during evolution. This review discusses the nature, biological role in host protection and potential biotechnological uses of some of these compounds, focusing on those from fish, marine invertebrates and marine micro-algae.

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          Antibacterial free fatty acids: activities, mechanisms of action and biotechnological potential.

          Andrew P Desbois, Valerie J Smith (2010)
          Amongst the diverse and potent biological activities of free fatty acids (FFAs) is the ability to kill or inhibit the growth of bacteria. The antibacterial properties of FFAs are used by many organisms to defend against parasitic or pathogenic bacteria. Whilst their antibacterial mode of action is still poorly understood, the prime target of FFA action is the cell membrane, where FFAs disrupt the electron transport chain and oxidative phosphorylation. Besides interfering with cellular energy production, FFA action may also result from the inhibition of enzyme activity, impairment of nutrient uptake, generation of peroxidation and auto-oxidation degradation products or direct lysis of bacterial cells. Their broad spectrum of activity, non-specific mode of action and safety makes them attractive as antibacterial agents for various applications in medicine, agriculture and food preservation, especially where the use of conventional antibiotics is undesirable or prohibited. Moreover, the evolution of inducible FFA-resistant phenotypes is less problematic than with conventional antibiotics. The potential for commercial or biomedical exploitation of antibacterial FFAs, especially for those from natural sources, is discussed.
          Article 0 comments Cited 343 times – based on 0 reviews     Review now
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            Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions.

            C Park, H Kim, S. C. Kim (1998)
            The mechanism of action of buforin II, which is a 21-amino acid peptide with a potent antimicrobial activity against a broad range of microorganisms, was studied using fluorescein isothiocyanate (FITC)-labeled buforin II and a gel-retardation experiment. Its mechanism of action was compared with that of the well-characterized magainin 2, which has a pore-forming activity on the cell membrane. Buforin II killed Esche-richia coli without lysing the cell membrane even at 5 times minimal inhibitory concentration (MIC) at which buforin II reduced the viable cell numbers by 6 orders of magnitude. However, magainin 2 lysed the cell to death under the same condition. FITC-labeled buforin II was found to penetrate the cell membrane and accumulate inside E. coli even below its MIC, whereas FITC-labeled magainin 2 remained outside or on the cell wall even at its MIC. The gel-retardation experiment showed that buforin II bound to DNA and RNA of the cells over 20 times strongly than magainin 2. All these results indicate that buforin II inhibits the cellular functions by binding to DNA and RNA of cells after penetrating the cell membranes, resulting in the rapid cell death, which is quite different from that of magainin 2 even though they are structurally similar: a linear amphipathic alpha-helical peptide.
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              Phagocytosis-independent antimicrobial activity of mast cells by means of extracellular trap formation.

              Maren von Köckritz-Blickwede, Oliver Goldmann, Pontus Thulin … (2008)
              These days it has been increasingly recognized that mast cells (MCs) are critical components of host defense against pathogens. In this study, we have provided the first evidence that MCs can kill bacteria by entrapping them in extracellular structures similar to the extracellular traps described for neutrophils (NETs). We took advantage of the ability of MCs to kill the human pathogen Streptococcus pyogenes by a phagocytosis-independent mechanism in order to characterize the extracellular antimicrobial activity of MCs. Close contact of bacteria and MCs was required for full antimicrobial activity. Immunofluorescence and electron microscopy revealed that S pyogenes was entrapped by extracellular structures produced by MCs (MCETs), which are composed of DNA, histones, tryptase, and the antimicrobial peptide LL-37. Disruption of MCETs significantly reduced the antimicrobial effect of MCs, suggesting that intact extracellular webs are critical for effective inhibition of bacterial growth. Similar to NETs, production of MCETs was mediated by a reactive oxygen species (ROS)-dependent cell death mechanism accompanied by disruption of the nuclear envelope, which can be induced after stimulation of MCs with phorbol-12-myristate-13-acetate (PMA), H(2)O(2), or bacterial pathogens. Our study provides the first experimental evidence of antimicrobial extracellular traps formation by an immune cell population other than neutrophils.
              Article 0 comments Cited 196 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Mar Drugs
                Journal ID (publisher-id): MD
                Title: Marine Drugs
                Publisher: Molecular Diversity Preservation International
                ISSN (Electronic): 1660-3397
                Publication date Collection: 2010
                Publication date (Electronic): 14 April 2010
                Volume: 8
                Issue: 4
                Pages: 1213-1262
                Affiliations
                [1 ] Scottish Oceans Institute, formerly the Gatty Marine Laboratory, University of St Andrews, St Andrews, KY16 8LB, Scotland, UK
                [2 ] Biomedical Sciences Research Complex, University of St Andrews, St Andrews, KY16 9ST, Scotland, UK
                [3 ] Centre for Marine Biodiversity and Biotechnology, School of Life Sciences, Heriot Watt University, Edinburgh, EH14 4AS, Scotland, UK
                Author notes
                * Author to whom correspondence should be addressed; E-Mail: vjs1@ 123456st-andrews.ac.uk ; Tel.: +44 (0) 1334 463474; Fax: +44 (0) 1334 463443.
                Article
                Publisher ID: marinedrugs-08-01213
                DOI: 10.3390/md8041213
                PMC ID: 2866484
                PubMed ID: 20479976
                SO-VID: 1f323213-d86a-4ecf-b4eb-215ec9dabf90
                Copyright © © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland
                License:

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 8 February 2010
                Date revision received : 2 April 2010
                Date accepted : 12 April 2010
                Categories
                Subject: Review

                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: pigments,fatty acids,antimicrobial peptides,innate defence,amphipathicity
                Data availability:
                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: pigments, fatty acids, antimicrobial peptides, innate defence, amphipathicity

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