NR AUXM
AU Aguzzi,A.
TI Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis.
QU Journal of Neurochemistry 2006 Jun; 97(6): 1726-39
PT journal article; review
AB 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 PrPsc or PrP-res, which represents a conformational isomer of the ubiquitous surface protein PrPc. 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.
ZR 153
MH Animal Diseases/epidemiology/genetics/pathology; Animals; Animals, Domestic; Creutzfeldt-Jakob Syndrome/epidemiology/genetics/veterinary; Disease Transmission; Humans; *Prion Diseases/epidemiology/genetics/pathology; Prions/*pathogenicity
AD Institute of Neuropathology, Universitätsspital Zürich, Zürich, Switzerland. adriano@pathol.unizh.ch
SP englisch
PO England