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@ARTICLE{Arad:613873,
      author       = {Arad, Elad and Pedersen, Kasper B. and Malka, Orit and
                      Mambram Kunnath, Sisira and Golan, Nimrod and Aibinder,
                      Polina and Schiøtt, Birgit and Rapaport, Hanna and Landau,
                      Meytal and Jelinek, Raz},
      title        = {{S}taphylococcus aureus functional amyloids catalyze
                      degradation of β-lactam antibiotics},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-05652},
      pages        = {8198},
      year         = {2023},
      abstract     = {Antibiotic resistance of bacteria is considered one of the
                      most alarming developments in modern medicine. While varied
                      pathways for bacteria acquiring antibiotic resistance have
                      been identified, there still are open questions concerning
                      the mechanisms underlying resistance. Here, we show that
                      alpha phenol-soluble modulins (PSMαs), functional bacterial
                      amyloids secreted by Staphylococcus aureus, catalyze
                      hydrolysis of β-lactams, a prominent class of antibiotic
                      compounds. Specifically, we show that PSMα2 and,
                      particularly, PSMα3 catalyze hydrolysis of the amide-like
                      bond of the four membered β-lactam ring of nitrocefin, an
                      antibiotic β-lactam surrogate. Examination of the catalytic
                      activities of several PSMα3 variants allowed mapping of the
                      active sites on the amyloid fibrils’ surface, specifically
                      underscoring the key roles of the cross-α fibril
                      organization, and the combined electrostatic and
                      nucleophilic functions of the lysine arrays. Molecular
                      dynamics simulations further illuminate the structural
                      features of β-lactam association upon the fibril surface.
                      Complementary experimental data underscore the generality of
                      the functional amyloid-mediated catalytic phenomenon,
                      demonstrating hydrolysis of clinically employed β-lactams
                      by PSMα3 fibrils, and illustrating antibiotic degradation
                      in actual S. aureus biofilms and live bacteria environments.
                      Overall, this study unveils functional amyloids as catalytic
                      agents inducing degradation of β-lactam antibiotics,
                      underlying possible antibiotic resistance mechanisms
                      associated with bacterial biofilms.},
      cin          = {CSSB-F / EMBL},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-F-20230420 / I:(DE-H253)EMBL-20120731},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38081813},
      UT           = {WOS:001142897900014},
      doi          = {10.1038/s41467-023-43624-1},
      url          = {https://bib-pubdb1.desy.de/record/613873},
}