NR AHHB
AU Liberski,P.P.; Bratosiewicz-Zapart,J.
TI Is the prion structure solved?
QU Archivum Immunologiae et Therapiae Experimentalis 1997; 45(2-3): 121-40
PT journal article; review; review, academic
AB We report here on the current knowledge on the nature of the scrapie agent or prion. Several lines of evidence suggest that the abnormal isoform of prion protein (PrP) is crucial for scrapie infectivity while evidence that PrP is also a part of the entire particle of the scrapie agent (prion) is much weaker. There is no doubt, however, that conformational changes (transitions from alpha-helical into beta-pleated structures) of PrP underlay scrapie pathogenesis. In view of the notorious puzzling nature of the scrapie agent, the electron microscopic search for the ultrastructural correlate of it is still warranted. Thus, we discuss the nature of tubulovesicular structures (TVS), the only diseases-specific particles known so far and the association between TVS and PrP fibrils which was recently discovered.
ZR 169
MH Amyloid/analysis; Animal; Cattle; Cerebral Amyloid Angiopathy/etiology/pathology; Encephalopathy, Bovine Spongiform/etiology/pathology; Goat Diseases/etiology/pathology; Goats; Hamsters; Human; Kuru/metabolism/pathology; Mice; Mice, Inbred C57BL; Mice, Transgenic; Microscopy, Electron; Models, Biological; PrP 27-30 Protein/chemistry/genetics; PrPsc Proteins/chemistry/genetics; Prion Diseases/etiology/*pathology/veterinary; Prions/*chemistry/genetics; *Protein Conformation; Scrapie/etiology/pathology; Sheep; Support, Non-U.S. Gov't
AD Department of Oncology, University Medical School, Lodz, Poland.
SP englisch
PO Polen