1. Novel prion protein conformation and glycotype in Creutzfeldt-Jakob disease.
- Author
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Zanusso G, Polo A, Farinazzo A, Nonno R, Cardone F, Di Bari M, Ferrari S, Principe S, Gelati M, Fasoli E, Fiorini M, Prelli F, Frangione B, Tridente G, Bentivoglio M, Giorgi A, Schininà ME, Maras B, Agrimi U, Rizzuto N, Pocchiari M, and Monaco S
- Subjects
- Aged, Animals, Arvicolinae, Brain metabolism, Brain pathology, Brain ultrastructure, Creutzfeldt-Jakob Syndrome genetics, Creutzfeldt-Jakob Syndrome transmission, Fatal Outcome, Female, Genotype, Glycosylation, Humans, Immunoblotting, Mass Spectrometry, Microscopy, Immunoelectron, Phenotype, PrP 27-30 Protein chemistry, PrP 27-30 Protein genetics, PrP 27-30 Protein metabolism, PrPSc Proteins chemistry, PrPSc Proteins genetics, Protein Conformation, Protein Structure, Tertiary, Creutzfeldt-Jakob Syndrome metabolism, PrPSc Proteins metabolism
- 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.
- Published
- 2007
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