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 PrPSc 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
ZANUSSO, Gianluigi;FARINAZZO, Alessia;FERRARI, Sergio;GELATI, Matteo;FIORINI, Michele;TRIDENTE, Giuseppe;BENTIVOGLIO FALES, Marina;RIZZUTO, Nicolo';MONACO, Salvatore
2007-01-01
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 PrPSc 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.