NR APIP
AU Käsermann,F.; Kempf,C.
TI Sodium hydroxide renders the prion protein PrPsc sensitive to proteinase K
QU Journal of General Virology 2003 Nov; 84(11): 3173-6
PT journal article
AB Sodium hydroxide (NaOH) solutions are widely used for the purification of contaminated equipment, as they are known to inactivate a variety of pathogens. However, information about their effect on agents causing transmissible spongiform encephalopathy (TSE) is sparse and contradictory. Scrapie hamster brain homogenate, containing the disease-associated form of the prion protein (PrPsc), was exposed to NaOH. Kinetics studies showed that treatment of brain homogenate with millimolar concentrations of NaOH rapidly abolished the proteinase K-resistant form of the prion protein (PrPres). NaOH treatment converted PrPsc into a protease-sensitive form, either in solution or when adsorbed to a metallic surface. If infectivity of TSEs is linked with PrPres, the results imply that inactivation of TSE occurs more efficiently than currently assumed.
MH Animals; *Decontamination; Endopeptidase K/*pharmacology; Hamsters; PrPsc Proteins/chemistry/*drug effects; Sodium Hydroxide/*pharmacology; Support, Non-U.S. Gov't
AD Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. kaessermann@ibc.unibe.ch
SP englisch
PO England