NR AWYO
AU 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.; Schinina,M.E.; Maras,B.; Agrimi,U.; Rizzuto,N.; Pocchiari,M.; Monaco,S.
TI Novel prion protein conformation and glycotype in Creutzfeldt-Jakob disease
QU Archives of Neurology 2007 Apr; 64(4): 595-9
PT case reports; journal article; research support, non-u.s. gov't
AB 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.
MH Aged; Animals; Arvicolinae; Brain/metabolism/pathology/ultrastructure; Creutzfeldt-Jakob Syndrome/genetics/*metabolism/transmission; Fatal Outcome; Female; Genotype; Glycosylation; Humans; Immunoblotting; Mass Spectrometry; Microscopy, Immunoelectron; Phenotype; PrP 27-30 Protein/chemistry/genetics/metabolism; PrPsc Proteins/chemistry/genetics/*metabolism; Protein Conformation; Protein Structure, Tertiary
AD Department of Neurologic, University of Verona, Verona, Italy.
SP englisch
PO USA