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@ARTICLE{Weiler:906277,
      author       = {Weiler, Andrea J. and Spitz, Olivia and Gudzuhn, Mirja and
                      Schott, Stephan and Kamel, Michael and Thiele, Björn and
                      Streit, Wolfgang R. and Kedrov, Alexej and Schmitt, Lutz and
                      Gohlke, Holger and Kovacic, Filip},
      title        = {{A} phospholipase {B} from {P}seudomonas aeruginosa with
                      activity towards endogenous phospholipids affects biofilm
                      assembly},
      journal      = {Biochimica et biophysica acta / Molecular and cell biology
                      of lipids},
      volume       = {1867},
      number       = {4},
      issn         = {1388-1981},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2022-01341},
      pages        = {159101 -},
      year         = {2022},
      abstract     = {Pseudomonas aeruginosa is a severe threat to
                      immunocompromised patients due to its numerous virulence
                      factors and biofilm-mediated multidrug resistance. It
                      produces and secretes various toxins with hydrolytic
                      activities including phospholipases. However, the function
                      of intracellular phospholipases for bacterial virulence has
                      still not been established. Here, we demonstrate that the
                      hypothetical gene pa2927 of P. aeruginosa encodes a novel
                      phospholipase B named PaPlaB. At reaction equilibrium,
                      PaPlaB purified from detergent-solubilized membranes of E.
                      coli released fatty acids (FAs) from sn-1 and sn-2 positions
                      of phospholipids at the molar ratio of 51:49. PaPlaB in
                      vitro hydrolyzed P. aeruginosa phospholipids reconstituted
                      in detergent micelles and phospholipids reconstituted in
                      vesicles. Cellular localization studies indicate that PaPlaB
                      is a cell-bound PLA of P. aeruginosa and that it is
                      peripherally bound to both membranes in E. coli, yet the
                      active form was predominantly associated with the
                      cytoplasmic membrane of E. coli. Decreasing the
                      concentration of purified and detergent-stabilized PaPlaB
                      leads to increased enzymatic activity, and at the same time
                      triggers oligomer dissociation. We showed that the free FA
                      profile, biofilm amount and architecture of the wild type
                      and ΔplaB differ. However, it remains to be established how
                      the PLB activity of PaPlaB is regulated by
                      homooligomerisation and how it relates to the phenotype of
                      the P. aeruginosa ΔplaB. This novel putative virulence
                      factor contributes to our understanding of phospholipid
                      degrading enzymes and might provide a target for new
                      therapeutics against P. aeruginosa biofilms.},
      cin          = {IMET / JSC / IBI-7 / NIC / IBG-4 / IBG-2 / IBG-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)IBG-2-20101118 /
                      I:(DE-Juel1)IBG-3-20101118},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / 5111 - Domain-Specific
                      Simulation $\&$ Data Life Cycle Labs (SDLs) and Research
                      Groups (POF4-511) / 5241 - Molecular Information Processing
                      in Cellular Systems (POF4-524) / 2173 - Agro-biogeosystems:
                      controls, feedbacks and impact (POF4-217) / Forschergruppe
                      Gohlke $(hkf7_20200501)$ / DFG project 267205415 - SFB 1208:
                      Identität und Dynamik von Membransystemen - von Molekülen
                      bis zu zellulären Funktionen (267205415)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(DE-HGF)POF4-5111 /
                      G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-2173 /
                      $G:(DE-Juel1)hkf7_20200501$ / G:(GEPRIS)267205415},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35063652},
      UT           = {WOS:000797596200005},
      doi          = {10.1016/j.bbalip.2021.159101},
      url          = {https://juser.fz-juelich.de/record/906277},
}