Decontamination of prion protein (BSE301V) using a genetically engineered protease

J. Dickinson, H. Murdoch, Michael Dennis, Graham Hall, R. Bott, W. D. Crabb, C. Penet, J. M. Sutton, N. D.H. Raven

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

A previous study has demonstrated the potential of alkaline proteases to inactivate bovine spongiform encephalopathy (BSE301V). Here we explored the use of MC3, a genetically engineered variant of Bacillus lentus subtilisin. MC3 was used to digest BSE301V infectious mouse brain homogenate (iMBH). MC3 eliminated all detectable 6H4-immunoreactive material at pH 10 and 12; however, Proteinase K was only partially effective at pH 12. When bioassayed in VM mice, MC3- and Proteinase K-digested iMBH gave respectively 66.6% and 22.7% survival rates. Using a titration series for disease incubation, this equates to a >7 log reduction in infectivity for MC3 and >6 log reduction for Proteinase K. This study demonstrates the potential for thermostable proteases to be developed as effective inactivation processes for prion agents in healthcare management. Crown

Original languageEnglish
Pages (from-to)65-70
Number of pages6
JournalJournal of Hospital Infection
Volume72
Issue number1
DOIs
Publication statusPublished - May 2009

Keywords

  • Bacillus lentus subtilisin
  • Bovine spongiform encephalopathy
  • Inactivation processes
  • Variant Creutzfeldt-Jakob disease

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