Abstract
Thermostable proteases have been investigated for their ability to provide a novel biological solution to decontamination of prion agents responsible for transmissible spongiform encephalopathies (TSEs). Proteases were identified that digested total mouse brain homogenate (MBH) protein from uninfected mice. These proteases were then evaluated for digestion of BSE (301V) infectious MBH over a range of pH and temperatures, screened for loss of anti-prion antibody 6H4 immunoreactivity and protease-treated infectious MBH assessed in mouse bioassay using VM mice. Despite a number of proteases eliminating all 6H4-immunoreactive material, only the subtilisin-enzyme Properase showed a significant extension in incubation period in mouse bioassays following a 30-min incubation at 60°C and pH 12. These results demonstrate the potential of the method to provide a practical solution to the problems of TSE contamination of surgical instruments and highlight the inadequacy of using Western blot for assessment of decontamination/inactivation of TSE agents.
| Original language | English |
|---|---|
| Pages (from-to) | 1165-1170 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 317 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 14 May 2004 |
Bibliographical note
Funding Information:Work was funded by grants from the EC (Contract BIO4-98-6065) and DEFRA (Contract SE 0224). We gratefully acknowledge the collaborators, Professor G. Antranikian, Professor M. Rossi, commercial suppliers for the provision of proteases, Dr. Brian Jones from Genencor International, Leiden, for useful discussions, and the skilful assistance of the Biological Investigation Group.
Keywords
- Creutzfeldt-Jakob disease
- Decontamination
- Meat rendering
- Prion
- Protease
- Surgical instruments
- Thermophile
- Transmissible spongiform encephalopathy