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@ARTICLE{Michalek:139939,
      author       = {Michalek, Matthias and Sönnichsen, Frank D and
                      Wechselberger, Rainer and Dingley, Andrew and Hung,
                      Chien-Wen and Kopp, Annika and Wienk, Hans and Simanski,
                      Maren and Herbst, Rosa and Lorenzen, Inken and
                      Marciano-Cabral, Francine and Gelhaus, Christoph and
                      Gutsmann, Thomas and Tholey, Andreas and Grötzinger,
                      Joachim and Leippe, Matthias},
      title        = {{S}tructure and function of a unique pore-forming protein
                      from a pathogenic acanthamoeba},
      journal      = {Nature Chemical Biology},
      volume       = {9},
      number       = {1},
      issn         = {1552-4469},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2013-05906},
      pages        = {37 - 42},
      year         = {2013},
      abstract     = {Human pathogens often produce soluble protein toxins that
                      generate pores inside membranes, resulting in the death of
                      target cells and tissue damage. In pathogenic amoebae, this
                      has been exemplified with amoebapores of the enteric
                      protozoan parasite Entamoeba histolytica. Here we
                      characterize acanthaporin, to our knowledge the first
                      pore-forming toxin to be described from acanthamoebae, which
                      are free-living, bacteria-feeding, unicellular organisms
                      that are opportunistic pathogens of increasing importance
                      and cause severe and often fatal diseases. We isolated
                      acanthaporin from extracts of virulent Acanthamoeba
                      culbertsoni by tracking its pore-forming activity,
                      molecularly cloned the gene of its precursor and
                      recombinantly expressed the mature protein in bacteria.
                      Acanthaporin was cytotoxic for human neuronal cells and
                      exerted antimicrobial activity against a variety of
                      bacterial strains by permeabilizing their membranes. The
                      tertiary structures of acanthaporin's active monomeric form
                      and inactive dimeric form, both solved by NMR spectroscopy,
                      revealed a currently unknown protein fold and a pH-dependent
                      trigger mechanism of activation.},
      cin          = {ICS-6},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000312484200010},
      pubmed       = {pmid:23143413},
      doi          = {10.1038/nchembio.1116},
      url          = {https://juser.fz-juelich.de/record/139939},
}