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      Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

      review-article
      Author(s): ,
      Publication date (Electronic):
      Journal: RNA Biology
      Publisher: Taylor & Francis
      Keywords: Lipid aminoacylation, antimicrobial resistance, cationic antimicrobial peptides, tRNA

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          ABSTRACT

          tRNA-dependent addition of amino acids to lipids on the outer surface of the bacterial membrane results in decreased effectiveness of antimicrobials such as cationic antimicrobial peptides (CAMPs) that target the membrane, and increased virulence of several pathogenic species. After a brief introduction to CAMPs and the various bacterial resistance mechanisms used to counteract these compounds, this review focuses on recent advances in tRNA-dependent pathways for lipid modification in bacteria. Phenotypes associated with amino acid lipid modifications and regulation of their expression will also be discussed.

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          Peptidoglycan structure and architecture.

          Waldemar Vollmer, Didier Blanot, Miguel de Pedro (2008)
          The peptidoglycan (murein) sacculus is a unique and essential structural element in the cell wall of most bacteria. Made of glycan strands cross-linked by short peptides, the sacculus forms a closed, bag-shaped structure surrounding the cytoplasmic membrane. There is a high diversity in the composition and sequence of the peptides in the peptidoglycan from different species. Furthermore, in several species examined, the fine structure of the peptidoglycan significantly varies with the growth conditions. Limited number of biophysical data on the thickness, elasticity and porosity of peptidoglycan are available. The different models for the architecture of peptidoglycan are discussed with respect to structural and physical parameters.
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            AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense.

            Yuping Lai, Richard Gallo (2009)
            Antimicrobial peptides (AMPs) are widely expressed and rapidly induced at epithelial surfaces to repel assault from diverse infectious agents including bacteria, viruses, fungi and parasites. Much information suggests that AMPs act by mechanisms that extend beyond their capacity to serve as gene-encoded antibiotics. For example, some AMPs alter the properties of the mammalian membrane or interact with its receptors to influence diverse cellular processes including cytokine release, chemotaxis, antigen presentation, angiogenesis and wound healing. These functions complement their antimicrobial action and favor resolution of infection and repair of damaged epithelia. Opposing this, some microbes have evolved mechanisms to inactivate or avoid AMPs and subsequently become pathogens. Thus, AMPs are multifunctional molecules that have a central role in infection and inflammation.
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              The co-evolution of host cationic antimicrobial peptides and microbial resistance.

              Andreas Peschel, Hans-Georg Sahl (2006)
              Endogenous cationic antimicrobial peptides (CAMPs) are among the most ancient and efficient components of host defence. It is somewhat of an enigma that bacteria have not developed highly effective CAMP-resistance mechanisms, such as those that inhibit many therapeutic antibiotics. Here, we propose that CAMPs and CAMP-resistance mechanisms have co-evolved, leading to a transient host-pathogen balance that has shaped the existing CAMP repertoire. Elucidating the underlying principles of this process could help in the development of more sustainable antibiotics.
              Article 0 comments Cited 255 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): RNA Biol
                Journal ID (iso-abbrev): RNA Biol
                Journal ID (publisher-id): KRNB
                Journal ID (publisher-id): krnb20
                Title: RNA Biology
                Publisher: Taylor & Francis
                ISSN (Print): 1547-6286
                ISSN (Electronic): 1555-8584
                Publication date Collection: 2018
                Publication date (Electronic): 3 November 2017
                Publication date PMC-release: 3 November 2017
                Volume: 15
                Issue: 4-5 , tRNA evolution and function
                Pages: 480-491
                Affiliations
                Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida , Orlando, Florida, United States of America
                Author notes
                CONTACT Hervé Roy Herve.Roy@ 123456ucf.edu Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida , 12722 Research Parkway, Orlando, Florida 32826, USA
                Article
                Publisher ID: 1356980
                DOI: 10.1080/15476286.2017.1356980
                PMC ID: 6103681
                PubMed ID: 28816600
                SO-VID: 8c6e6d86-2466-445f-aeb1-e7fa4f144b98
                Copyright © © 2018 The Author(s). Published with license by Taylor & Francis Group, LLC
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License ( http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

                History
                Date received : 24 May 2017
                Date revision received : 11 July 2017
                Date accepted : 12 July 2017
                Page count
                Figures: 7, Tables: 0, Equations: 0, References: 118, Pages: 12
                Categories
                Subject: Review - Solicited

                ScienceOpen disciplines: Molecular biology
                Keywords: lipid aminoacylation,antimicrobial resistance,cationic antimicrobial peptides,trna
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: lipid aminoacylation, antimicrobial resistance, cationic antimicrobial peptides, trna

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