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@ARTICLE{Karbelkar:614011,
      author       = {Karbelkar, Amruta A. and Font, Maria and Smith, T. Jarrod
                      and Sondermann, Holger and O’Toole, George A.},
      title        = {{R}econstitution of a biofilm adhesin system from a
                      sulfate-reducing bacterium in {P}seudomonas fluorescens},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {121},
      number       = {13},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {PUBDB-2024-05712},
      pages        = {e2320410121},
      year         = {2024},
      abstract     = {Biofilms of sulfate-reducing bacterium (SRB) like
                      Desulfovibrio vulgaris Hildenborough (DvH) can facilitate
                      metal corrosion in various industrial and environmental
                      settings leading to substantial economic losses. Although
                      the mechanisms of biofilm formation by DvH are not yet well
                      understood, recent studies indicate the large adhesin, DvhA,
                      is a key determinant of biofilm formation. The dvhA gene
                      neighborhood resembles the biofilm-regulating Lap system of
                      Pseudomonas fluorescens but is curiously missing the
                      c-di-GMP-binding regulator LapD. Instead, DvH encodes an
                      evolutionarily unrelated c-di-GMP-binding protein (DVU1020)
                      that we hypothesized is functionally analogous to LapD. To
                      study this unusual Lap system and overcome experimental
                      limitations with the slow-growing anaerobe DvH, we
                      reconstituted its predicted SRB Lap system in a P.
                      fluorescens strain lacking its native Lap regulatory
                      components (ΔlapGΔlapD). Our data support the model that
                      DvhA is a cell surface–associated LapA-like adhesin with a
                      N-terminal “retention module” and that DvhA is released
                      from the cell surface upon cleavage by the LapG-like
                      protease DvhG. Further, we demonstrate DVU1020 (named here
                      DvhD) represents a distinct class of c-di-GMP-binding,
                      biofilm-regulating proteins that regulates DvhG activity in
                      response to intracellular levels of this second messenger.
                      This study provides insight into the key players responsible
                      for biofilm formation by DvH, thereby expanding our
                      understanding of Lap-like systems.},
      cin          = {CSSB-DESY-HS},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-DESY-HS-20210521},
      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:38498718},
      UT           = {WOS:001208065700003},
      doi          = {10.1073/pnas.2320410121},
      url          = {https://bib-pubdb1.desy.de/record/614011},
}