Abstract
The only known difference between the cellular (PrP(C)) and scrapie- specific (PrP(Sc)) isoforms of the prion protein is conformational. Because disruption of PrP(Sc) structure decreases scrapie infectivity, restoration of the disease-specific conformation should restore infectivity. In this study, disruption of PrP(Sc) (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.
| Original language | English |
|---|---|
| Pages (from-to) | 25545-25547 |
| Number of pages | 3 |
| Journal | Journal of Biological Chemistry |
| Volume | 273 |
| Issue number | 40 |
| DOIs | |
| State | Published - Oct 2 1998 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
Cite this
Reversibility of scrapie inactivation is enhanced by copper. / McKenzie, Debbie; Bartz, Jason C.; Mirwald, Jean; Olander, Doris; Marsh, Richard; Aiken, Judd.
In: Journal of Biological Chemistry, Vol. 273, No. 40, 02.10.1998, p. 25545-25547.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Reversibility of scrapie inactivation is enhanced by copper
AU - McKenzie, Debbie
AU - Bartz, Jason C.
AU - Mirwald, Jean
AU - Olander, Doris
AU - Marsh, Richard
AU - Aiken, Judd
PY - 1998/10/2
Y1 - 1998/10/2
N2 - The only known difference between the cellular (PrP(C)) and scrapie- specific (PrP(Sc)) isoforms of the prion protein is conformational. Because disruption of PrP(Sc) structure decreases scrapie infectivity, restoration of the disease-specific conformation should restore infectivity. In this study, disruption of PrP(Sc) (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.
AB - The only known difference between the cellular (PrP(C)) and scrapie- specific (PrP(Sc)) isoforms of the prion protein is conformational. Because disruption of PrP(Sc) structure decreases scrapie infectivity, restoration of the disease-specific conformation should restore infectivity. In this study, disruption of PrP(Sc) (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.
UR - http://www.scopus.com/inward/record.url?scp=0032476035&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032476035&partnerID=8YFLogxK
U2 - 10.1074/jbc.273.40.25545
DO - 10.1074/jbc.273.40.25545
M3 - Article
C2 - 9748215
AN - SCOPUS:0032476035
VL - 273
SP - 25545
EP - 25547
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 40
ER -