title: Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.
abstract: 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).
authors.affiliation: Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana 59840, USA.
authors.forename: B
authors.initials: B
authors.lastname: Caughey
authors.forename: G J
authors.initials: GJ
authors.lastname: Raymond
authors.forename: D A
authors.initials: DA
authors.lastname: Kocisko
authors.forename: P T
authors.initials: PT
authors.lastname: Lansbury
mesh_terms: 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
chemical_list: D006146:Guanidines; D018620:PrPSc Proteins; D019286:Endopeptidase K; D019791:Guanidine