Genetic analysis of Creutzfeldt-Jakob disease and related disorders

Abstract
Genetic studies of over 200 cases of Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI) and kuru have brought a reliable body of evidence that the familial forms of cjd and all known cases of gss and ffi are linked to germline mutations in the coding region of the PRNP gene on chromosome 20, either point substitutions or expansion of the number of 24-nucleotide repeat units. Phenotypic expression of FFI and familial CJD, clinically and pathologically distinct syndromes linked to the 178Asp-->Asn substitution, is dependent on a polymorphism at codon 129. Synthetic peptides homologous to several regions of PrP spontaneously form insoluble amyloid fibrils with unique morphological characteristics and polymerization tendencies. Peptides homologous to mutated regions of PrP exhibit enhanced fibrillogenic properties and, if mixed with the wild-type peptide, produce even more abundant and larger fibrous aggregates. A similar process in vivo may be the primary event leading to amyloid accumulation and disease.

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