Which criteria best support the diagnosis of VV1 sporadic Creutzfeldt–Jakob disease?
Surachai Supattapone* and Judy R Rees
Correspondence *Department of Biochemistry, 7200 Vail Building, Dartmouth Medical School, Hanover, NH 03755, USA
Email surachai.supattapone@dartmouth.edu
This article has no abstract so we have provided the first paragraph of the full text.
Prion diseases are neurodegenerative diseases associated with the misfolding of a normal neuronal protein, PrPC, into an abnormal conformer, PrPSc. Human prion diseases occur in inherited, sporadic and infectious forms, and it is hypothesized that PrPSc is itself an infectious protein. sCJD, the most common form of human prion disease, exhibits a wide spectrum of clinical characteristics. The basis for this variation might be the existence of multiple PrPSc conformational states with different biochemical and pathogenic properties. Supporting this view, subgroups of sCJD patients with similar clinical profiles can be classified according to the PrP allotype at polymorphic codon 129 (methionine or valine) and the type of protease-digested PrPSc molecules in brain tissue (apparent molecular weight of 21 kDa or 19 kDa).1
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