Effects of Surfactant and a Hyperthermostable Protease on Infectivity of Scrapie-Infected Mouse Brain Homogenate | OMICS International | Abstract
ISSN: 2155-952X

Journal of Biotechnology & Biomaterials
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Research Article

Effects of Surfactant and a Hyperthermostable Protease on Infectivity of Scrapie-Infected Mouse Brain Homogenate

Azumi Hirata1,2, Akikazu Sakudo3, Kazufumi Takano1, Shigenori Kanaya4 and Yuichi Koga4*

1Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, 1-5 Hangi-cho, Shimogamo, Sakyo-ku, Japan

2Departments of Anatomy and Cell Biology, Faculty of Medicine, Osaka Medical College, 2-7 Daigaku-machi, Takatsuki, Japan

3Laboratory of Biometabolic Chemistry, School of Health Science, Faculty of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Japan

4Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Japan

Corresponding Author:
Yuichi Koga
Department of Material and Life Science
Graduate School of Engineering, Osaka University
2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
Tel: +81-6-6879-7443
Fax: +81-6-6879-7443
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.


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Citations : 1536

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