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@ARTICLE{Loschwitz:1015356,
      author       = {Loschwitz, Jennifer and Steffens, Nora and Wang, Xue and
                      Schäffler, Moritz and Pfeffer, Klaus and Degrandi, Daniel
                      and Strodel, Birgit},
      title        = {{D}omain motions, dimerization, and membrane interactions
                      of the murine guanylate binding protein 2},
      journal      = {Scientific reports},
      volume       = {13},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2023-03676},
      pages        = {679},
      year         = {2023},
      abstract     = {Guanylate-binding proteins (GBPs) are a group of GTPases
                      that are induced by interferon-γ and are crucial components
                      of cell-autonomous immunity against intracellular pathogens.
                      Here, we examine murine GBP2 (mGBP2), which we have
                      previously shown to be an essential effector protein for the
                      control of Toxoplasma gondii replication, with its
                      recruitment through the membrane of the parasitophorous
                      vacuole and its involvement in the destruction of this
                      membrane likely playing a role. The overall aim of our work
                      is to provide a molecular-level understanding of the mutual
                      influences of mGBP2 and the parasitophorous vacuole
                      membrane. To this end, we performed lipid-binding assays
                      which revealed that mGBP2 has a particular affinity for
                      cardiolipin. This observation was confirmed by fluorescence
                      microscopy using giant unilamellar vesicles of different
                      lipid compositions. To obtain an understanding of the
                      protein dynamics and how this is affected by GTP binding,
                      mGBP2 dimerization, and membrane binding, assuming that each
                      of these steps are relevant for the function of the protein,
                      we carried out standard as well as replica exchange
                      molecular dynamics simulations with an accumulated
                      simulation time of more than 30 μs. The main findings from
                      these simulations are that mGBP2 features a large-scale
                      hinge motion in its M/E domain, which is present in each of
                      the studied protein states. When bound to a
                      cardiolipin-containing membrane, this hinge motion is
                      particularly pronounced, leading to an up and down motion of
                      the M/E domain on the membrane, which did not occur on a
                      membrane without cardiolipin. Our prognosis is that this up
                      and down motion has the potential to destroy the membrane
                      following the formation of supramolecular mGBP2 complexes on
                      the membrane surface.},
      cin          = {IBI-7},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36639389},
      UT           = {WOS:000968670400028},
      doi          = {10.1038/s41598-023-27520-8},
      url          = {https://juser.fz-juelich.de/record/1015356},
}