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@INPROCEEDINGS{Wolf:145207,
      author       = {Wolf, Hanna and Pleschka, Catharina and Graßmann, Andrea
                      and Hossinger, Andre and Möhl, Christoph and Paulsen, Lydia
                      and Vorberg, Ina},
      title        = {{P}.16: {G}lycosaminoglycan modulationaffects cellular
                      prion replicationdownstream of {P}r{PS}c internalization},
      journal      = {Prion},
      volume       = {9},
      number       = {Suppelment 1},
      issn         = {1933-6896},
      reportid     = {DZNE-2020-00565},
      pages        = {S19},
      year         = {2015},
      abstract     = {Prions are unconventional infectious agentscomposed
                      primarily of misfolded aggregatedhost prion protein PrP,
                      termed PrPSc. Conversion of cellular prion protein into
                      PrPSc occurson the cell surface or along the endocytic
                      pathway. The precise mechanisms and cellularrequirements for
                      PrPSc uptake, the initial PrPScformation and the persistent
                      PrPSc propagationstill remain unknown.
                      Glycosaminoglycans(GAGs), highly-sulfated unbranched
                      polysaccharides present on the cell surface and
                      withinendocytic vesicles, have been implicated as
                      firstattachment sites for prions and cofactors for
                      replication. GAG mimetics and obstruction ofGAG sulfation
                      affect prion replication, but sofar, comparative analysis of
                      the role of GAGsduring the individual stages of infection by
                      22Lprion strain has not been performed. We examined the
                      effect of the GAG mimetic, DS-500,and the sulfation
                      inhibitor, NaClO3, on prioninfection by scrapie strain 22L
                      in L929 cellsand organotypic cerebellar slices. Here weshow
                      that both compounds change the cellulardistribution and
                      levels of sulfated GAGs buthave divergent effects on cell
                      surface and totalPrPC levels in L929 cells. Chemical
                      manipulation of GAGs did not prevent PrPSc uptake,arguing
                      against their role as essential attachment sites.
                      Importantly, GAG undersulfationand DS-500 effectively
                      antagonized de novoand chronic 22L prion infection in L929
                      cellsand organotypic cerebellar slices. We concludethat
                      DS-500 and NaClO3 affect events downstream of the initial
                      PrPSc attachment andinternalization.},
      month         = {May},
      date          = {2015-05-26},
      organization  = {International Prion Congress—Prion
                       2015, Atlanta, GA (USA), 26 May 2015 -
                       29 May 2015},
      cin          = {AG Vorberg / IDAF},
      ddc          = {570},
      cid          = {I:(DE-2719)1013004 / I:(DE-2719)1040200},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      experiment   = {EXP:(DE-2719)IDAF-20190308},
      typ          = {PUB:(DE-HGF)1 / PUB:(DE-HGF)16},
      url          = {https://pub.dzne.de/record/145207},
}