Review: Creutzfeldt-Jakob disease: prion protein type, disease phenotype and agent strain

• Published in: Neuropathology and applied neurobiology Vol. 38; no. 4; pp. 296 - 310
• Main Authors: Head, M. W., Ironside, J. W.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.06.2012; Blackwell
• Subjects: agent strain; Animals; Biological and medical sciences; Creutzfeldt-Jakob disease; Creutzfeldt-Jakob Syndrome - classification; Creutzfeldt-Jakob Syndrome - genetics; Creutzfeldt-Jakob Syndrome - pathology; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases; Humans; Medical sciences; Neurology; neuropathology; Phenotype; prion protein; Prions - chemistry; Prions - genetics; PRNP gene; protein misfolding disease; Prion disease; Nervous system diseases; Creutzfeldt-Jakob disease; agent strain; Review; protein misfolding disease; Cerebral disorder; Infection; PRNP gene; Phenotype; Gene; Central nervous system disease; Degenerative disease; Prion; Prion protein; neuropathology
• ISSN: 0305-1846; 1365-2990
• DOI: 10.1111/j.1365-2990.2012.01265.x

M. W. Head and J. W. Ironside (2012) Neuropathology and Applied Neurobiology38, 296–310 Creutzfeldt–Jakob disease: prion protein type, disease phenotype and agent strain The human transmissible spongiform encephalopathies or human prion diseases are one of the most intensively investigated groups of rare human neurodegenerative conditions. They are generally held to be unique in terms of their complex epidemiology and phenotypic variability, but they may also serve as a paradigm with which other more common protein misfolding disorders might be compared and contrasted. The clinico‐pathological phenotype of human prion diseases appears to depend on a complex interaction between the prion protein genotype of the affected individual and the physico‐chemical properties of the neurotoxic and transmissible agent, thought to comprise of misfolded prion protein. A major focus of research in recent years has been to define the phenotypic heterogeneity of the recognized human prion diseases, correlate this with molecular‐genetic features and then determine whether this molecular‐genetic classification of human prion disease defines the biological properties of the agent as determined by animal transmission studies. This review seeks to survey the field as it currently stands, summarize what has been learned, and explore what remains to be investigated in order to obtain a more complete scientific understanding of prion diseases and to protect public health.