ABSTRACT
Department of Neurology, University of Chicago Hospitals, Chicago, Illinois, U.S.A.
INTRODUCTION
Also known as transmissible spongiform encephalopathies (TSEs), and previously considered to result from a ‘‘slow virus,’’ this unique family of transmissible neurodegenerative disorders results from the accumulation within the brain of misfolded prion protein (PrP). Prion disease (PrD) is typified by its most common phenotype, Creutzfeldt-Jakob disease (CJD), which presents as a rapidly progressive dementia associated with ataxia and myoclonus; however, at least four other phenotypes are recognized, namely Gerstmann-Stra¨ussler-Scheinker disease (GSS), fatal insomnia (FI), new variant (v) CJD, and kuru. While the majority of cases occur on a sporadic basis, approximately 15% are associated with an autosomal dominant mutation within the PrP gene (PRNP), and a susceptibility polymorphism at codon 129 within PRNP appears to play a role in both. This chapter will review PrD, with special attention to the genetic aspects of disease.
HISTORICAL BACKGROUND
