Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K.

Käsermann F; Kempf C

doi:10.1099/vir.0.19355-0

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Journal article

Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K.

Käsermann F Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.
Kempf C ZLB Bioplasma AG, Bern, Switzerland.

2003-10-24

Published in:

The Journal of general virology. - 2003

English 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 (PrP(Sc)), 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 (PrP(res)). NaOH treatment converted PrP(Sc) into a protease-sensitive form, either in solution or when adsorbed to a metallic surface. If infectivity of TSEs is linked with PrP(res), the results imply that inactivation of TSE occurs more efficiently than currently assumed.

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