Effects of Surfactant and a Hyperthermostable Protease on Infectivity of Scrapie-Infected Mouse Brain HomogenateAzumi Hirata1,2, Akikazu Sakudo3, Kazufumi Takano1, Shigenori Kanaya4 and Yuichi Koga4*
- Corresponding Author:
- Yuichi Koga
Department of Material and Life Science
Graduate School of Engineering, Osaka University
2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
E-mail: [email protected]
Received date: July 22, 2015; Accepted date: August 25, 2015; Published date: August 31, 2015
Citation: Hirata A, Sakudo A, Takano K, Kanaya S, Koga Y (2015) Effects of Surfactant and a Hyperthermostable Protease on Infectivity of Scrapie-Infected Mouse Brain Homogenate. J Biotechnol Biomater 5:194. doi:10.4172/2155-952X.1000194
Copyright: © 2015 Hirata A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PrPSc is thought to be the infective agent of TSE, and inactivating the infectivity of PrPSc without using strong reagents is difficult. Although PrPSc is a protease resistant protein, it can be degraded in vitro by the hyperthermophilic protease (Tk-subtilisin) at temperatures above 65ºC through the synergistic effect of heat destabilization of PrP and the high proteolytic activity of the thermostable protease. However, the change in infectivity of the proteasedigested PrPSc is still unknown. Therefore, we used mouse brain homogenate containing PrPSc (SBH) in a bioassay to investigate the loss of infectivity after Tk-subtilisin digestion. Surprisingly, the Tk-subtilisin digested SBH retained a high level of infectivity. Despite this, Tk-subtilisin could still be used for decontamination in highly protein denaturing condition such as in the presence of SDS.