NR AOUQ
AU Käsermann,F.; Kempf,C.
TI Sodium Hydroxide Renders the Prion Protein PrPsc Proteinase K Sensitive
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - BR-21
PT Konferenz-Poster
AB Sodium hydroxide solutions are widely used for purification of contaminated equipment. They are known to inactivate a variety of pathogens. However, information about their effect on the 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 sodium hydroxide. Kinetic studies showed that treatment of brain homogenate with NaOH in the millimolar range 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.
AD Fabian Käsermann, Christoph Kempf, University of Bern, Switzerland
SP englisch
PO Deutschland