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@ARTICLE{KausDrobek:632992,
      author       = {Kaus-Drobek, Magdalena and Nowacka, Marzena and
                      Gewartowska, Magdalena and Korzeniowska nee Wiweger,
                      Małgorzata and Jensen, Merete Rusås and Møretrø, Trond
                      and Heir, Even and Nowak, Elżbieta and Sabała, Izabela},
      title        = {{F}rom discovery to potential application: engineering a
                      novel {M}23 peptidase to combat {L}isteria monocytogenes},
      journal      = {Scientific reports},
      volume       = {15},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2025-02318},
      pages        = {15628},
      year         = {2025},
      abstract     = {Peptidoglycan hydrolases are promising alternatives for
                      combating pathogens due to their specificity and potent
                      bacteriolytic activity. In this study, a novel M23 peptidase
                      from Streptococcus thermophilus NCTC10353, designated StM23,
                      was discovered and characterized. It exhibited antibacterial
                      activity against Listeria monocytogenes and other
                      Gram-positive bacteria with meso-DAP-type peptidoglycan,
                      including Bacillus subtilis and Bacillus cereus. To enhance
                      StM23’s efficacy and specificity, a chimeric enzyme,
                      $StM23_CWT,$ was engineered by fusing its catalytic domain
                      with a cell wall-targeting domain (CWT) from SpM23B, a
                      peptidoglycan hydrolase found in Staphylococcus
                      pettenkoferi. The engineered chimera demonstrated expanded
                      specificity, showing activity against Staphylococcus aureus
                      and Enterococcus faecium. Its ability to disrupt L.
                      monocytogenes cells was visualized by electron microscopy.
                      The enzyme effectively disrupted biofilm structures and
                      decontaminated surfaces like glass, stainless steel, and
                      silicone, showcasing its industrial potential. Safety
                      evaluations using zebrafish, moth larvae, and human cell
                      models confirmed its non-toxic profile, supporting its broad
                      applicability. Based on these findings, $StM23_CWT$ is a
                      novel and potent antimicrobial agent with significant
                      potential to reduce the risk of listeriosis and control
                      persistent pathogens.},
      cin          = {EMBL-User},
      ddc          = {600},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40325189},
      doi          = {10.1038/s41598-025-99141-2},
      url          = {https://bib-pubdb1.desy.de/record/632992},
}