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@ARTICLE{Kuhle:207429,
      author       = {Kuhle, K. and Krausze, J. and Curth, U. and Roessle,
                      Manfred and Heuner, K. and Lang, C. and Flieger, A.},
      title        = {{O}ligomerization {I}nhibits {L}egionella {P}neumophila
                      {P}la{B} {P}hospholipase {A} {A}ctivity},
      journal      = {The journal of biological chemistry},
      volume       = {289},
      number       = {27},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PUBDB-2015-01339},
      pages        = {18657 - 18666},
      year         = {2014},
      note         = {(c) by The American Society for Biochemistry and Molecular
                      Biology, Inc. Post referee full text in progress.},
      abstract     = {The intracellularly replicating lung pathogen Legionella
                      pneumophila consists of an extraordinary variety of
                      phospholipases, including at least 15 different
                      phospholipases A (PLA). Among them, PlaB, the first
                      characterized member of a novel lipase family, is a
                      hemolytic virulence factor that exhibits the most prominent
                      PLA activity in L. pneumophila. We analyzed here protein
                      oligomerization, the importance of oligomerization for
                      activity, addressed further essential regions for activity
                      within the PlaB C terminus, and the significance of
                      PlaB-derived lipolytic activity for L. pneumophila
                      intracellular replication. We determined by means of
                      analytical ultracentrifugation and small angle x-ray
                      scattering analysis that PlaB forms homodimers and
                      homotetramers. The C-terminal 5, 10, or 15 amino acids,
                      although the individual regions contributed to PLA activity,
                      were not essential for protein tetramerization. Infection of
                      mouse macrophages with L. pneumophila wild type, plaB
                      knock-out mutant, and plaB complementing or various mutated
                      plaB-harboring strains showed that catalytic activity of
                      PlaB promotes intracellular replication. We observed that
                      PlaB was most active in the lower nanomolar concentration
                      range but not at or only at a low level at concentration
                      above 0.1 $\mu M$ where it exists in a dimer/tetramer
                      equilibrium. We therefore conclude that PlaB is a virulence
                      factor that, on the one hand, assembles in inactive
                      tetramers at micromolar concentrations. On the other hand,
                      oligomer dissociation at nanomolar concentrations activates
                      PLA activity. Our data highlight the first example of
                      concentration-dependent phospholipase inactivation by
                      tetramerization, which may protect the bacterium from
                      internal PLA activity, but enzyme dissociation may allow its
                      activation after export.},
      cin          = {EMBL / DOOR},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)HAS-User-20120731},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13) / 6G3 - PETRA III
                      (POF3-622)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405 / G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101 / EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000339062900004},
      doi          = {10.1074/jbc.M114.573196},
      url          = {https://bib-pubdb1.desy.de/record/207429},
}