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These plaque-like deposits were mostly non-congophilic and consists of full-length, uncleaved PrP, indicating retention of this glycophosphatidylinositol (GPI) anchor. Prion aggregates sedimented in reduced density fractions after ultracentrifugation, in line with oligomers, and bound lower levels of heparan sulfate (HS) comparable to other predominantly GPI-anchored prions. Collectively, these outcomes suggest that highly glycosylated PrP mainly converts as a GPI-a

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