NR ACJP
AU Caughey,B.W.; Raymond,G.J.; Kocisko,D.A.; Lansbury,P.T.Jr.
TI Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies
QU Journal of Virology 1997 May; 71(5): 4107-10
PT journal article
AB Denaturation studies with guanidine HCl (GdnHCl) were performed to test the relationship between scrapie infectivity and properties of scrapie-associated prion protein (PrPsc). Large GdnHCl-induced reductions in infectivity were associated with the irreversible elimination of both the proteinase K resistance and apparent self-propagating converting activity of PrPsc. In intermediate GdnHCl concentrations that stimulate converting activity and partially disaggregate PrPsc, both scrapie infectivity and converting activity were associated with residual partially protease-resistant multimers of PrPsc.
MH Animal; Endopeptidase K/pharmacology; Guanidine; Guanidines/*pharmacology; Hamsters; Mesocricetus; PrPsc Proteins/drug effects/*toxicity; Protein Denaturation
AD Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana 59840, USA
SP englisch
PO USA
OR Prion-Krankheiten C