Concentration and distribution of infectivity and PrPSc following partial denaturation of a mouse-adapted and a hamster-adapted scrapie strain.
PrPSc is a specific protein marker for slow infectious diseases known as the transmissible subacute spongiform encephalopathies. Although PrPSc is closely associated with infectivity, it is not known if it is the infectious agent itself, a component of the agent or merely adventitiously associated with infectivity. In the present study we demonstrate that the resistance of PrPSc to partial denaturation and of infectivity to inactivation differs markedly for two scrapie strains. Proteinase K treatment or electrophoretic analysis of partially denatured PrPSc preparations reveal a dissociation between infectivity and demonstrable PrPSc. Our findings support other evidence that not all PrPSc is required for infectivity. Our studies combined with previous biological analyses suggest that PrPSc cannot be the sole component associated with the infectious agent.
NYS Institute for Basic Research in Developmental Disabilities, Staten Island, New York.
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Rubenstein
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Carp
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Ju
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Scalici
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Papini
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Rubenstein
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Kascsak
D000818:Animals; D015153:Blotting, Western; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K; D006358:Hot Temperature; D008623:Mercaptoethanol / Q000494:pharmacology; D051379:Mice; D018620:PrPSc Proteins / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification / Q000472:pathogenicity*; D011489:Protein Denaturation; D012608:Scrapie / Q000821:virology; D012697:Serine Endopeptidases / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology
D018620:PrPSc Proteins; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol; D012697:Serine Endopeptidases; D019286:Endopeptidase K