The partially proteinase resistant form of the prion protein (PrPsc) is thought to be the causative agent of transmissible spongiform encephalopathies (TSE, e.g. BSE). PrPsc is one of the most stable proteins known. According to WHO recommendation inactivation of this protein requires incubation with 2M NaOH for > 1hr.
New studies in our lab imply a revision of the old view on decontamination of TSE. Treatment with sodium hydroxide converted PrPsc into a protease sensitive form either in solution or when adsorbed to a metallic surface. PrPsc can be destroyed with low concentration of sodium hydroxide. This implies that the inactivation of TSE occurs much faster and more readily than previously assumed. These results will have consequences on the decontamination procedures currently in use (e.g, surgery instruments).

This work was carried out in the group of Prof. Christoph Kempf.

References:

• F. Käsermann, C. Kempf;
  "Sodium hydroxide renders the prion protein PrPsc sensitive to proteinase K"
  J. Gen. Virol., 84, 3173-3176, (2003); doi:10.1099/vir.0.19355-0.