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@ARTICLE{Bannach:202091,
      author       = {Bannach, Oliver and Birkmann, Eva and Reinartz, Elke and
                      Jaeger, Karl-Erich and Langeveld, Jan P. M. and Rohwer,
                      Robert G. and Gregori, Luisa and Terry, Linda A. and
                      Willbold, Dieter and Riesner, Detlev},
      title        = {{D}etection of {P}rion {P}rotein {P}articles in {B}lood
                      {P}lasma of {S}crapie {I}nfected {S}heep},
      journal      = {PLoS one},
      volume       = {7},
      number       = {5},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-04380},
      pages        = {e36620 -},
      year         = {2012},
      abstract     = {Prion diseases are transmissible neurodegenerative diseases
                      affecting humans and animals. The agent of the disease is
                      the prion consisting mainly, if not solely, of a misfolded
                      and aggregated isoform of the host-encoded prion protein
                      (PrP). Transmission of prions can occur naturally but also
                      accidentally, e.g. by blood transfusion, which has raised
                      serious concerns about blood product safety and emphasized
                      the need for a reliable diagnostic test. In this report we
                      present a method based on surface-FIDA (fluorescence
                      intensity distribution analysis), that exploits the high
                      state of molecular aggregation of PrP as an unequivocal
                      diagnostic marker of the disease, and show that it can
                      detect infection in blood. To prepare PrP aggregates from
                      blood plasma we introduced a detergent and lipase treatment
                      to separate PrP from blood lipophilic components. Prion
                      protein aggregates were subsequently precipitated by
                      phosphotungstic acid, immobilized on a glass surface by
                      covalently bound capture antibodies, and finally labeled
                      with fluorescent antibody probes. Individual PrP aggregates
                      were visualized by laser scanning microscopy where signal
                      intensity was proportional to aggregate size. After signal
                      processing to remove the background from low fluorescence
                      particles, fluorescence intensities of all remaining PrP
                      particles were summed. We detected PrP aggregates in plasma
                      samples from six out of ten scrapie-positive sheep with no
                      false positives from uninfected sheep. Applying simultaneous
                      intensity and size discrimination, ten out of ten samples
                      from scrapie sheep could be differentiated from uninfected
                      sheep. The implications for ante mortem diagnosis of prion
                      diseases are discussed.},
      cin          = {ICS-6},
      ddc          = {500},
      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:000305341500089},
      pubmed       = {pmid:22567169},
      doi          = {10.1371/journal.pone.0036620},
      url          = {https://juser.fz-juelich.de/record/202091},
}