Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K.
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.
Käsermann
Fabian
F
Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.
Kempf
Christoph
C
ZLB Bioplasma AG, Bern, Switzerland.|Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.
D000818:Animals; D006224:Cricetinae; D003666:Decontamination; D019286:Endopeptidase K / Q000494:pharmacology*; D018620:PrPSc Proteins / Q000737:chemistry / Q000187:drug effects*; D012972:Sodium Hydroxide / Q000494:pharmacology*
D018620:PrPSc Proteins; D012972:Sodium Hydroxide; D019286:Endopeptidase K