Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.
Denaturation studies with guanidine HCl (GdnHCl) were performed to test the relationship between scrapie infectivity and properties of scrapie-associated prion protein (PrP(Sc)). 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 PrP(Sc). In intermediate GdnHCl concentrations that stimulate converting activity and partially disaggregate PrP(Sc), both scrapie infectivity and converting activity were associated with residual partially protease-resistant multimers of PrP(Sc).
Caughey
B
B
Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana 59840, USA.
Raymond
G J
GJ
Kocisko
D A
DA
Lansbury
P T
PT
D000818:Animals; D006224:Cricetinae; D019286:Endopeptidase K / Q000494:pharmacology; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology*; D008647:Mesocricetus; D018620:PrPSc Proteins / Q000187:drug effects / Q000633:toxicity*; D011489:Protein Denaturation
D006146:Guanidines; D018620:PrPSc Proteins; D019286:Endopeptidase K; D019791:Guanidine