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      A Pilot Study of the Synergy between Two Antimicrobial Peptides and Two Common Antibiotics

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          Abstract

          Background: Frequent and unrestricted use of antibiotics has been associated with the development of antibiotic resistance by microorganisms. Thus, there is a need to find novel antibacterial agents or a combination of agents as the first line of treatment for various infections. This study aimed to investigate the synergy between antimicrobial peptide (AMP) combinations or between AMP-antibiotics combinations using two common pathogens, Pseudomonas aeruginosa and Staphylococcus aureus. Methods: The AMPs melimine, Mel4 and protamine, and antibiotics cefepime and ciprofloxacin were used in this study. The minimum inhibitory concentration (MIC) of each were evaluated against P. aeruginosa and S. aureus strains by a microtiter broth dilution. Based on the MIC of each antimicrobial agent, a checkerboard assay was performed to investigate the synergy between them, which was expressed as the fractional inhibitory concentration (FIC). Results: The combination of melimine and ciprofloxacin showed synergistic activity against antibiotic sensitive or resistant strains of P. aeruginosa and with FIC values ≤0.5. Conclusion: Combinations of AMPs and the fluoroquinolone ciprofloxacin is a promising method for reducing resistance to the fluoroquinolone of P. aeruginosa.

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          DNA gyrase, topoisomerase IV, and the 4-quinolones.

          K Drlica, X. Zhao (1997)
          For many years, DNA gyrase was thought to be responsible both for unlinking replicated daughter chromosomes and for controlling negative superhelical tension in bacterial DNA. However, in 1990 a homolog of gyrase, topoisomerase IV, that had a potent decatenating activity was discovered. It is now clear that topoisomerase IV, rather than gyrase, is responsible for decatenation of interlinked chromosomes. Moreover, topoisomerase IV is a target of the 4-quinolones, antibacterial agents that had previously been thought to target only gyrase. The key event in quinolone action is reversible trapping of gyrase-DNA and topoisomerase IV-DNA complexes. Complex formation with gyrase is followed by a rapid, reversible inhibition of DNA synthesis, cessation of growth, and induction of the SOS response. At higher drug concentrations, cell death occurs as double-strand DNA breaks are released from trapped gyrase and/or topoisomerase IV complexes. Repair of quinolone-induced DNA damage occurs largely via recombination pathways. In many gram-negative bacteria, resistance to moderate levels of quinolone arises from mutation of the gyrase A protein and resistance to high levels of quinolone arises from mutation of a second gyrase and/or topoisomerase IV site. For some gram-positive bacteria, the situation is reversed: primary resistance occurs through changes in topoisomerase IV while gyrase changes give additional resistance. Gyrase is also trapped on DNA by lethal gene products of certain large, low-copy-number plasmids. Thus, quinolone-topoisomerase biology is providing a model for understanding aspects of host-parasite interactions and providing ways to investigate manipulation of the bacterial chromosome by topoisomerases.
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            Mechanisms of ciprofloxacin resistance in Pseudomonas aeruginosa: new approaches to an old problem

            Attika Rehman, Wayne Patrick, Iain Lamont (2019)
            The antibiotic ciprofloxacin is used extensively to treat a wide range of infections caused by the opportunistic pathogen Pseudomonas aeruginosa. Due to its extensive use, the proportion of ciprofloxacin-resistant P. aeruginosa isolates is rapidly increasing. Ciprofloxacin resistance can arise through the acquisition of mutations in genes encoding the target proteins of ciprofloxacin and regulators of efflux pumps, which leads to overexpression of these pumps. However, understanding of the basis of ciprofloxacin resistance is not yet complete. Recent advances using high-throughput screens and experimental evolution combined with whole-genome sequencing and protein analysis are enhancing our understanding of the genetic and biochemical mechanisms involved in ciprofloxacin resistance. Better insights into the mechanisms of ciprofloxacin resistance may facilitate the development of new or improved therapeutic regimes effective against P. aeruginosa. In this review we discuss the current understanding of the mechanisms of ciprofloxacin resistance and summarize the genetic basis of ciprofloxacin resistance in P. aeruginosa, in the context of current and future use of this antibiotic.
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              Efflux-mediated resistance to fluoroquinolones in gram-negative bacteria.

              K. Poole (2000)
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                Author and article information

                Journal
                Journal ID (nlm-ta): Antibiotics (Basel)
                Journal ID (iso-abbrev): Antibiotics (Basel)
                Journal ID (publisher-id): antibiotics
                Title: Antibiotics
                Publisher: MDPI
                ISSN (Electronic): 2079-6382
                Publication date (Electronic): 09 May 2019
                Publication date Collection: June 2019
                Volume: 8
                Issue: 2
                Electronic Location Identifier: 60
                Affiliations
                [1 ]School of Life Science, Engineering & Design, Saxion University of Applied Science, 7513 AB Enschede, The Netherlands; franziska.kampshoff@ 123456gmx.de
                [2 ]School of Optometry and Vision Science, University of New South Wales, Sydney, NSW 2052, Australia; duttadebarun@ 123456gmail.com
                [3 ]Ophthalmic Research Group, Optometry School, Aston University, Birmingham B4 7ET, UK
                Author notes
                [* ]Correspondence: m.willcox@ 123456unsw.edu.au
                Author information
                https://orcid.org/0000-0003-3842-7563
                Article
                Publisher ID: antibiotics-08-00060
                DOI: 10.3390/antibiotics8020060
                PMC ID: 6627861
                PubMed ID: 31075940
                SO-VID: 79ad5df6-125a-44f9-bc05-a9cea715a2f1
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 26 March 2019
                Date accepted : 05 May 2019
                Categories
                Subject: Article

                Keywords: synergy,antimicrobial peptides,antibiotics,staphylococcus,pseudomonas
                Data availability:
                Keywords: synergy, antimicrobial peptides, antibiotics, staphylococcus, pseudomonas

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