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      The Stability, and Efficacy Against Penicillin-Resistant Enterococcus faecium, of the Plectasin Peptide Efficiently Produced by Escherichia coli.

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          Abstract

          Plectasin, the first defensin extracted from a fungus (the saprophytic ascomycete Pseudoplectania nigrella), is attractive as a prospective antimicrobial agent. The purpose of this study was to establish a bacterium-based production system and evaluate the antimicrobial activity of the resulting plectasin. A gene encoding plectasin, with the codon preference of Escherichia coli, was optimized based on its amino acid sequence, synthesized using gene-splicing with overlap extension PCR, and inserted into the expression vector pGEX-4T-1. The fusion protein was expressed in the soluble fraction of E. coli and purified using glutathione Stransferase affinity chromatography. Plectasin was cleaved from the fusion protein with thrombin and purified by ultrafiltration. The purified plectasin showed strong, concentration-dependent antimicrobial activity against gram-positive bacteria, including antibiotic-resistant bacteria, especially penicillin-resistant Enterococcus faecium. This antimicrobial activity was equal to chemically synthesized plectasin and was maintained over a wide range of pH and temperatures. This soluble recombinant expression system in E. coli is effective for producing plectasin at a relatively lower cost, and higher purity and efficiency than prior systems, and might provide a foundation for developing a large-scale production system. Overall, plectasin shows potential as a novel, high-performance, and safe antibiotic for the treatment of refractory diseases caused by drug-resistant bacterial strains.

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          Author and article information

          Journal
          J Microbiol Biotechnol
          Journal of microbiology and biotechnology
          Journal of Microbiology and Biotechnology
          1738-8872
          1017-7825
          Jul 2015
          : 25
          : 7
          Affiliations
          [1 ] Department of Respiratory Medicine, Zhujiang Hospital, Southern Medical University, Guangzhou 510282, P.R. China.
          [2 ] Nanfang Hospital, First Clinical Medical College, Southern Medical University, Guangzhou 510515, P.R. China.
          [3 ] Biosafety Level-3 Laboratory, School of Public Health and Tropical Medicine, Southern Medical University, Guangzhou 510515, P.R. China.
          [4 ] Department of Respiratory Diseases, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou 510120, P.R. China.
          Article
          10.4014/jmb.1501.01056
          10.4014/jmb.1501.01056
          25791854
          46a705d1-03da-4a29-9fb0-74840289fba7
          History

          Antimicrobial peptide,antimicrobial activity,fusion protein

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