NR AXDW
AU Aguzzi,A.; Heikenwalder,M.; Polymenidou,M.
TI Insights into prion strains and neurotoxicity
QU Nature Reviews. Molecular Cell Biology 2007 Jul; 8(7): 552-61
PT journal article; research support, non-u.s. gov't; review
AB Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases that are caused by prions and affect humans and many animal species. It is now widely accepted that the infectious agent that causes TSEs is PrPsc, an aggregated moiety of the host-derived membrane glycolipoprotein PrPc. Although PrPc is encoded by the host genome, prions themselves encipher many phenotypic TSE variants, known as prion strains. Prion strains are TSE isolates that, after inoculation into distinct hosts, cause disease with consistent characteristics, such as incubation period, distinct patterns of PrPsc distribution and spongiosis and relative severity of the spongiform changes in the brain. The existence of such strains poses a fascinating challenge to prion research.
ZR 137
MH Amino Acid Sequence; Animals; Brain/metabolism/*pathology; Conserved Sequence; Creutzfeldt-Jakob Syndrome/etiology/metabolism/pathology; Disease Transmission, Horizontal; Forecasting; Glycosylation; Humans; Incidence; Models, Biological; Molecular Sequence Data; PrPsc Proteins/chemistry/genetics/isolation &; purification/metabolism/*pathogenicity/*toxicity; Prion; Diseases/classification/epidemiology/etiology/pathology/transmission/veter; inary; Prions/chemistry/*genetics/metabolism/*pathogenicity/*toxicity; Protein Sorting Signals; Protein Structure, Secondary; Scrapie/pathology/transmission; Species Specificity; Tissue Distribution; Variation (Genetics)
AD Institute of Neuropathology, University Hospital of Zürich, Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland. adriano.aguzzi@usz.ch
SP englisch
PO England