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@ARTICLE{Golan:613872,
      author       = {Golan, Nimrod and Parizat, Amit and Tabachnikov, Orly and
                      Barnea, Eilon and Olsen, William P. and Otzen, Daniel E. and
                      Landau, Meytal},
      title        = {{R}esilience and {C}harge-{D}ependent {F}ibrillation of
                      {F}unctional {A}myloids: {I}nteractions of {P}seudomonas
                      {B}iofilm-{A}ssociated {F}ap{B} and {F}ap{C}},
      reportid     = {PUBDB-2024-05651},
      year         = {2024},
      abstract     = {FapC and FapB are biofilm-associated amyloids involved in
                      the virulence of Pseudomonas and other bacteria. We herein
                      demonstrate their exceptional thermal and chemical
                      resilience, suggesting that biofilm structures might
                      withstand standard sterilization, thereby contributing to
                      the persistence of P. aeruginosa infections. Our findings
                      also underscore the impact of environmental factors on Fap
                      proteins, suggesting that orthologs in different Pseudomonas
                      strains adapt to specific environments and roles.
                      Challenging previous assumptions about a simple nucleation
                      role for FapB in promoting FapC aggregation, the study shows
                      a significant influence of FapC on FapB aggregation. The
                      interaction between FapB and FapC is intricate: FapB
                      stabilizes FapC fibrils, while FapC slows down FapB
                      fibrillation but can still serve as a cross-seeding
                      template. This complex interplay is key to understanding
                      their roles in bacterial biofilms. Furthermore, the study
                      highlights distinct differences between Fap and E. coli’s
                      curli CsgA amyloid, where CsgB assumes a simple
                      unidirectional role in nucleating CsgA fibrillation,
                      emphasizing the importance of a comprehensive understanding
                      of various amyloid systems. This knowledge is vital for
                      developing effective intervention strategies against
                      bacterial infections and leveraging the unique properties of
                      these amyloids in technological applications such as novel
                      bio-nanomaterials or protective coatings.},
      cin          = {CSSB-F},
      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)25},
      doi          = {10.1101/2024.02.14.580233},
      url          = {https://bib-pubdb1.desy.de/record/613872},
}