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      Bacteriocins: Properties and potential use as antimicrobials

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          Abstract

          A variety of bacteriocins originate from lactic acid bacteria, which have recently been modified by scientists. Many strains of lactic acid bacteria related to food groups could produce bacteriocins or antibacterial proteins highly effective against foodborne pathogens such as Staphylococcus aureus, Pseudomonas fluorescens, P. aeruginosa, Salmonella typhi, Shigella flexneri, Listeria monocytogenes, Escherichia coli O157:H7, and Clostridium botulinum. A wide range of bacteria belonging primarily to the genera Bifidobacterium and Lactobacillus have been characterized with different health‐promoting attributes. Extensive studies and in‐depth understanding of these antimicrobials mechanisms of action could enable scientists to determine their production in specific probiotic lactic acid bacteria, as they are potentially crucial for the final preservation of functional foods or for medicinal applications. In this review study, the structure, classification, mode of operation, safety, and antibacterial properties of bacteriocins as well as their effect on foodborne pathogens and antibiotic‐resistant bacteria were extensively studied.

          Abstract

          Antimicrobial potential of bacteiocins in food preservation.

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          Most cited references280

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          Histone methyltransferase activity of a Drosophila Polycomb group repressor complex.

          Polycomb group (PcG) proteins maintain transcriptional repression during development, likely by creating repressive chromatin states. The Extra Sex Combs (ESC) and Enhancer of Zeste [E(Z)] proteins are partners in an essential PcG complex, but its full composition and biochemical activities are not known. A SET domain in E(Z) suggests this complex might methylate histones. We purified an ESC-E(Z) complex from Drosophila embryos and found four major subunits: ESC, E(Z), NURF-55, and the PcG repressor, SU(Z)12. A recombinant complex reconstituted from these four subunits methylates lysine-27 of histone H3. Mutations in the E(Z) SET domain disrupt methyltransferase activity in vitro and HOX gene repression in vivo. These results identify E(Z) as a PcG protein with enzymatic activity and implicate histone methylation in PcG-mediated silencing.
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            Colicin biology.

            Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.
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              Human commensals producing a novel antibiotic impair pathogen colonization.

              The vast majority of systemic bacterial infections are caused by facultative, often antibiotic-resistant, pathogens colonizing human body surfaces. Nasal carriage of Staphylococcus aureus predisposes to invasive infection, but the mechanisms that permit or interfere with pathogen colonization are largely unknown. Whereas soil microbes are known to compete by production of antibiotics, such processes have rarely been reported for human microbiota. We show that nasal Staphylococcus lugdunensis strains produce lugdunin, a novel thiazolidine-containing cyclic peptide antibiotic that prohibits colonization by S. aureus, and a rare example of a non-ribosomally synthesized bioactive compound from human-associated bacteria. Lugdunin is bactericidal against major pathogens, effective in animal models, and not prone to causing development of resistance in S. aureus. Notably, human nasal colonization by S. lugdunensis was associated with a significantly reduced S. aureus carriage rate, suggesting that lugdunin or lugdunin-producing commensal bacteria could be valuable for preventing staphylococcal infections. Moreover, human microbiota should be considered as a source for new antibiotics.
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                Author and article information

                Contributors
                R.Ghanavati@behums.ac.ir , Qanavati.r@gmail.com
                Maryam_kakanj@yahoo.com
                Journal
                J Clin Lab Anal
                J Clin Lab Anal
                10.1002/(ISSN)1098-2825
                JCLA
                Journal of Clinical Laboratory Analysis
                John Wiley and Sons Inc. (Hoboken )
                0887-8013
                1098-2825
                01 December 2021
                January 2022
                : 36
                : 1 ( doiID: 10.1002/jcla.v36.1 )
                : e24093
                Affiliations
                [ 1 ] Department of Microbiology School of Medicine Iran University of Medical Sciences Tehran Iran
                [ 2 ] Microbial Biotechnology Research Centre Iran University of Medical Sciences Tehran Iran
                [ 3 ] Department of Pathobiology School of Public Health Tehran University of Medical Sciences Tehran Iran
                [ 4 ] Behbahan Faculty of Medical Sciences Behbahan Iran
                [ 5 ] Food and Drug Laboratory Research Center Food and Drug Administration MOH&ME Tehran Iran
                Author notes
                [*] [* ] Correspondence

                Roya Ghanavati, Behbahan Faculty of Medical Sciences, Shahid Zibaei street, Behbahan, Khouzestan Province, Iran.

                Emails: R.Ghanavati@ 123456behums.ac.ir ; Qanavati.r@ 123456gmail.com

                Maryam Kakanj, Food and Drug Laboratory Research Center, Food and Drug Administation, MOH&ME, Tehran, Iran.

                Email: Maryam_kakanj@ 123456yahoo.com

                Author information
                https://orcid.org/0000-0002-3851-0001
                Article
                JCLA24093
                10.1002/jcla.24093
                8761470
                34851542
                68cbc241-e2b2-42e3-893e-d6f9c3f50cbb
                © 2021 The Authors. Journal of Clinical Laboratory Analysis published by Wiley Periodicals LLC.

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 03 October 2021
                : 09 August 2021
                : 24 October 2021
                Page count
                Figures: 1, Tables: 9, Pages: 8, Words: 24959
                Funding
                Funded by: Behbahan Faculty of medical sciences
                Award ID: 99052
                Categories
                Review Article
                Review Article
                Custom metadata
                2.0
                January 2022
                Converter:WILEY_ML3GV2_TO_JATSPMC version:6.7.0 mode:remove_FC converted:16.01.2022

                Clinical chemistry
                bacteriocin,foodborne pathogens,lactic acid bacteria
                Clinical chemistry
                bacteriocin, foodborne pathogens, lactic acid bacteria

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