Details

Autor(en) / Beteiligte

• Koga, Yuichi
• Tanaka, Shun-ichi
• Sakudo, Akikazu
• Tobiume, Minoru
• Aranishi, Mutsuo
• Hirata, Azumi
• Takano, Kazufumi
• Ikuta, Kazuyoshi
• Kanaya, Shigenori

Titel

Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1

Ist Teil von

• Applied microbiology and biotechnology, 2014-03, Vol.98 (5), p.2113-2120

Ort / Verlag

Berlin/Heidelberg: Springer-Verlag

Erscheinungsjahr

2014

Quelle

MEDLINE

Beschreibungen/Notizen

• The abnormal prion protein (scrapie-associated prion protein, PrPSᶜ) is considered to be included in the group of infectious agents of transmissible spongiform encephalopathies. Since PrPSᶜ is highly resistant to normal sterilization procedures, the decontamination of PrPSᶜ is a significant public health issue. In the present study, a hyperthermostable protease, Tk-subtilisin, was used to degrade PrPSᶜ. Although PrPSᶜ is known to be resistant toward proteolytic enzymes, Tk-subtilisin was able to degrade PrPSᶜ under extreme conditions. The level of PrPSᶜ in brain homogenates was found to decrease significantly in vitro following Tk-subtilisin treatment at 100 °C, whereas some protease-resistant fractions remain after proteinase K treatment. Rather small amounts of Tk-subtilisin (0.3 U) were required to degrade PrPSᶜ at 100 °C and pH 8.0. In addition, Tk-subtilisin was observed to degrade PrPSᶜ in the presence of sodium dodecyl sulfate or other industrial surfactants. Although several proteases degrading PrPSᶜ have been reported, practical decontamination procedures using enzymes are not available. This report aims to provide basic information for the practical use of a proteolytic enzyme for PrPSᶜ degradation.