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@ARTICLE{Rayan:598542,
      author       = {Rayan, Bader and Barnea, Eilon and Khokhlov, Alexander and
                      Upcher, Alexander and Landau, Meytal},
      title        = {{D}ifferential fibril morphologies and thermostability
                      determine functional roles of {S}taphylococcus aureus
                      {PSM}$α$1 and {PSM}$α$3},
      journal      = {Frontiers in molecular biosciences},
      volume       = {10},
      issn         = {2296-889X},
      address      = {Lausanne},
      publisher    = {Frontiers},
      reportid     = {PUBDB-2023-06862},
      pages        = {1184785},
      year         = {2023},
      abstract     = {Phenol-soluble modulins (PSMs) are virulent peptides
                      secreted by staphylococci that undergo self-assembly into
                      amyloid fibrils. This study focuses on Staphylococcus aureus
                      PSMα1 and PSM$α$3, which share homologous sequences but
                      exhibit distinct amyloid fibril structures. Upon subjecting
                      PSMα1 to an 80°C heat shock, it fibrillates into cross-β
                      structures, resulting in the loss of cytotoxic activity.
                      Conversely, PSM$α$3 cross-α fibrils undergo reversible
                      disaggregation upon heat shock, leading to the recovery of
                      cytotoxicity. The differential thermostability probably
                      arises from the presence of hydrogen bonds along the
                      β-strands within the β-sheets of the cross-β fibrils. We
                      propose that the breakdown of PSM$α$3 fibrils into soluble
                      species, potentially co-aggregating with membrane lipids, is
                      crucial for its toxic process and enables the reversible
                      modulation of its biological activity under stress
                      conditions. In contrast, the formation of robust and
                      irreversible cross-β fibrils by PSM$α$1 corresponds to its
                      role in biofilm stability. These findings emphasize how the
                      unique fibril morphologies and thermostability of PSMα1 and
                      PSM$α$3 shape their functional roles in various
                      environments of S. aureus.},
      cin          = {CSSB-F},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-F-20230420},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37469708},
      UT           = {WOS:001028851000001},
      doi          = {10.3389/fmolb.2023.1184785},
      url          = {https://bib-pubdb1.desy.de/record/598542},
}