Glycidol Degrades Scrapie Mouse Prion Protein

Journal of Veterinary Medical Science

Naotaka ISHIGURO¹  Mari YAMAMOTO¹  Takato MATSUO²  Morikazu SHINAGAWA¹  Kenji KANEKO²  Motohiro HORIUCHI¹ 

[1] Laboratory of Veterinary Public Health, Department of Veterinary Medicine, Obihiro University of Agriculture and Veterinary Medicine;Tokyo Research Laboratory, Nihon Pharmaceutical Co., Ltd.

关键词: decontamination;    gycidol;    prion;    scrapie;   

DOI  :  10.1292/jvms.63.983

学科分类：兽医学

来源: Japanese Society of Veterinary Science

【 摘 要 】

References(22)Cited-By(4)Agents of transmissible spongiform encephalopathy (prion) are known to be extremely resistant to physicochemical inactivation procedures such as heat, radiation, chemical disinfectants such as detergents, alcohols, glutaraldehyde, formalin, and so on. Because of its remarkable resistance, it is difficult to inactivate prion. Chemical inactivation seems to be a practical method because it is applicable to large or fixed surfaces and complicated equipment. Here, three epoxides: β-propiolactone, propylene oxide, and glycidol (GLD) were examined of their inactivation ability against scrapie-mouse prion protein (PrPSc) under various conditions of chemical concentration, incubation time, and temperature. Among these chemicals, GLD worked most effectively and degraded PrP into small fragments. As a result of the bioassay, treatment with 3% GLD for 5 hr and 5% GLD for 2, 5 hr or 12 hr at room temperature prolonged the mean incubation time by 44, 30, 110 and 73 days, respectively. From dose-incubation time standard curve, the decrease in infectivity titers were estimated as 103 or more. Therefore, degradation of PrPSc by GLD decreased the scrapie infectivity. It is also suggested that pH and salt concentrations influence the effect of GLD. Although further study is necessary to determine the optimal condition, GLD may be a potential prion disinfectant.

【 授权许可】

Unknown