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