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J Biol Chem, Vol. 273, Issue 40, 25545-25547, October 2, 1998
From the Department of Animal Health and Biomedical Sciences,
University of Wisconsin-Madison, Madison, Wisconsin 53706
The only known difference between the cellular
(PrPC) and scrapie-specific (PrPSc)
isoforms of the prion protein is conformational. Because disruption of
PrPSc structure decreases scrapie infectivity, restoration
of the disease-specific conformation should restore infectivity. In
this study, disruption of PrPSc (as monitored by the loss
of proteinase K resistance) by guanidine hydrochloride (GdnHCl)
resulted in decreased infectivity. Upon dilution of the GdnHCl,
protease resistance of PrP was restored and infectivity was regained.
The addition of copper facilitated restoration of both infectivity and
protease resistance of PrP in a subset of samples that did not renature
by the simple dilution of the GdnHCl. These data demonstrate that loss
of scrapie infectivity can be a reversible process and that copper can
enhance this restoration of proteinase K resistance and
infectivity.
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