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Novel Prion Protein Conformation and Glycotype in Creutzfeldt-Jakob Disease

2007; American Medical Association; Volume: 64; Issue: 4 Linguagem: Inglês

10.1001/archneur.64.4.595

1538-3687

Gianluigi Zanusso, Alberto Polo, Alessia Farinazzo, Romolo Nonno, Franco Cardone, Michele Di Bari, Sérgio Ferrari, Serena Principe, Matteo Gelati, Elisa Fasoli, Michele Fiorini, Frances Prelli, Blas Frangione, Giuseppe Tridente, Marina Bentivoglio, Alessandra Giorgi, Maria Eugenia Schininà, Bruno Maras, Umberto Agrimi, Nicola Rizzuto, Maurizio Pocchiari, Salvatore Monaco,

Neurological diseases and metabolism

Objective To describe a novel molecular and pathological phenotype of Creutzfeldt-Jakob disease. Patient A 69-year-old woman with behavioral and personality changes followed by rapidly evolving dementia. Results Postmortem examination of the brain showed intracellular prion protein deposition and axonal swellings filled with amyloid fibrils. Biochemical analysis of the pathological prion protein disclosed a previously unrecognized PrP Sc tertiary structure lacking diglycosylated species. Genetic analysis revealed a wild-type prion protein gene. The prion agent responsible for this atypical phenotype was successfully passaged to bank voles. Conclusion To our knowledge, our results define a new human prion disorder characterized by intracellular accumulation of a novel type of pathological prion protein.