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.
Novel prion protein conformation and glycotype in Creutzfeldt-Jakob disease / Gianluigi, Zanusso; Alberto, Polo; Alessia, Farinazzo; Romolo, Nonno; Franco, Cardone; Michele Di, Bari; Sergio, Ferrari; Serena, Principe; Matteo, Gelati; Elisa, Fasoli; Michele, Fiorini; Frances, Prelli; Blas, Frangione; Giuseppe, Tridente; Marina, Bentivoglio; Giorgi, Alessandra; Schinina', Maria Eugenia; Maras, Bruno; Umberto, Agrimi; Nicola, Rizzuto; Maurizio, Pocchiari; Salvatore, Monaco. - In: ARCHIVES OF NEUROLOGY. - ISSN 0003-9942. - STAMPA. - 64:4(2007), pp. 595-599. [10.1001/archneur.64.4.595]
Novel prion protein conformation and glycotype in Creutzfeldt-Jakob disease
GIORGI, ALESSANDRA;SCHININA', Maria Eugenia;MARAS, Bruno;
2007
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
