Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis.
Neuronal vacuolation (spongiosis), neuronal death, and pronounced glial reactions are the hallmarks of transmissible spongiform encephalopathies (TSEs), or prion diseases. A wealth of physical, biochemical, and immunological evidence indicates that the TSE agent, termed prion, does not contain agent-specific nucleic acid encoding its own constituents, as is the case for all other infectious pathogens. Also, no adaptive immune responses are elicited upon infection. A defining feature of TSEs is the deposition, mainly in the brain and lymphoreticular tissues, of an aggregated and structurally abnormal protein, designated PrP(Sc) or PrP-res, which represents a conformational isomer of the ubiquitous surface protein PrP(C). Biochemical and genetic evidence link PrP and its gene to the disease. Although TSEs are by definition transmissible, a growing number of Prnp-associated non-infectious neurodegenerative proteinopathies are now being recognized.
Aguzzi
Adriano
A
Institute of Neuropathology, Universitätsspital Zürich, Zürich, Switzerland. adriano@pathol.unizh.ch
D000820:Animal Diseases / Q000453:epidemiology / Q000235:genetics / Q000473:pathology; D000818:Animals; D000829:Animals, Domestic; D007562:Creutzfeldt-Jakob Syndrome / Q000453:epidemiology / Q000235:genetics / Q000662:veterinary; D018562:Disease Transmission, Infectious; D006801:Humans; D017096:Prion Diseases / Q000453:epidemiology / Q000235:genetics / Q000473:pathology; D011328:Prions / Q000472:pathogenicity*
D011328:Prions