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      Purification, Characterization, and Mode of Action of Pentocin JL-1, a Novel Bacteriocin Isolated from Lactobacillus pentosus, against Drug-Resistant Staphylococcus aureus

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      BioMed Research International
      Hindawi

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          Abstract

          Staphylococcus aureus and its drug-resistant strains, which threaten public health and food safety, are in need of effective control by biopreservatives. A novel bacteriocin, pentocin JL-1, produced by Lactobacillus pentosus that was isolated from the intestinal tract of Chiloscyllium punctatum, was purified by a four-step chromatographic process. Mass spectrometry based on MALDI-TOF indicated that pentocin JL-1 has a molecular mass of 2987.23 Da. Only six of the twenty-five amino acids could be identified by Edman degradation. This bacteriocin is thermostable and tolerates a pH range of 5–7. Also, it is sensitive to proteinase K, trypsin, pepsin, and alkaline protease. This bacteriocin has a broad inhibitory spectrum against both Gram-positive and Gram-negative strains and in particular is effective against multidrug-resistant S. aureus. Additionally, we showed that the cell membrane is the target of pentocin JL-1 against methicillin-resistant S. aureus (MRSA), causing a loss of proton motive force. Furthermore, pentocin JL-1 has a drastic impact on the structure and integrity of MRSA cells. These results suggest that pentocin JL-1 has potential as a biopreservative in the food industry.

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          Bacteriocins of lactic acid bacteria: extending the family

          Lactic acid bacteria (LAB) constitute a heterogeneous group of microorganisms that produce lactic acid as the major product during the fermentation process. LAB are Gram-positive bacteria with great biotechnological potential in the food industry. They can produce bacteriocins, which are proteinaceous antimicrobial molecules with a diverse genetic origin, posttranslationally modified or not, that can help the producer organism to outcompete other bacterial species. In this review, we focus on the various types of bacteriocins that can be found in LAB and the organization and regulation of the gene clusters responsible for their production and biosynthesis, and consider the food applications of the prototype bacteriocins from LAB. Furthermore, we propose a revised classification of bacteriocins that can accommodate the increasing number of classes reported over the last years. Electronic supplementary material The online version of this article (doi:10.1007/s00253-016-7343-9) contains supplementary material, which is available to authorized users.
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            Role of membranes in the activities of antimicrobial cationic peptides.

            Cationic amphiphilic peptides that are found throughout nature have very broad-spectrum activities against microbes. The initial sites of interaction are with microbial membranes. Although dogma suggests that their lethal action involves disruption of the cytoplasmic membranes, a number of cationic peptides can traverse intact membranes to interact with internal targets.
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              Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.

              Antibacterial, membrane-lytic peptides belong to the innate immune system and host defense mechanism of a multitude of animals and plants. The largest group of peptide antibiotics comprises peptides which fold into an amphipathic alpha-helical conformation when interacting with the target. The activity of these peptides is thought to be determined by global structural parameters rather than by the specific amino acid sequence. This review is concerned with the influence of structural parameters, such as peptide helicity, hydrophobicity, hydrophobic moment, peptide charge and the size of the hydrophobic/hydrophilic domain, on membrane activity and selectivity. The potential of these parameters to increase the antibacterial activity and to improve the prokaryotic selectivity of natural and model peptides is assessed. Furthermore, biophysical studies are summarized which elucidated the molecular basis for activity and selectivity modulations on the level of model membranes. Finally, the knowledge about the role of peptide structural parameters is applied to understand the different activity spectra of natural membrane-lytic peptides.
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                Author and article information

                Contributors
                Journal
                Biomed Res Int
                Biomed Res Int
                BMRI
                BioMed Research International
                Hindawi
                2314-6133
                2314-6141
                2017
                29 November 2017
                : 2017
                : 7657190
                Affiliations
                Key Laboratory of Marine Food Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou, Zhejiang 310018, China
                Author notes

                Academic Editor: Pierluigi Di Ciccio

                Author information
                http://orcid.org/0000-0002-1733-8345
                Article
                10.1155/2017/7657190
                5733122
                f7c7f058-a31b-4347-a058-ac5eca0a0d0a
                Copyright © 2017 Han Jiang et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 6 June 2017
                : 21 September 2017
                : 18 October 2017
                Funding
                Funded by: Natural Science Foundation of Zhejiang Province
                Award ID: LQ18C200004
                Award ID: LQ17C200002
                Funded by: Application Research Program of Commonweal Technology of Zhejiang Province, China
                Award ID: 2016C37083
                Award ID: 2016C32064
                Funded by: National Natural Science Foundation of China
                Award ID: 31601464
                Categories
                Research Article

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