Glycidol degrades scrapie mouse prion protein

Citation
M. Yamamoto et al., Glycidol degrades scrapie mouse prion protein, J VET MED S, 63(9), 2001, pp. 983-990
Citations number
22
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Veterinary Medicine/Animal Health
Journal title
JOURNAL OF VETERINARY MEDICAL SCIENCE
ISSN journal
0916-7250 → ACNP
Volume
63
Issue
9
Year of publication
2001
Pages
983 - 990
Database
ISI
SICI code
0916-7250(200109)63:9<983:GDSMPP>2.0.ZU;2-4
Abstract
Agents of transmissible spongiform encephalopathy (prion) are known to be e xtremely resistant to physicochemical inactivation procedures such as heat, radiation, chemical disinfectants such as detergents, alcohols, glutaralde hyde, formalin, and so on. Because of its remarkable resistance, it is diff icult to inactivate prion. Chemical inactivation seems to be a practical me thod because it is applicable to large or fixed surfaces and complicated eq uipment. Here, three epoxides: beta -propiolactone, propylene oxide, and gl ycidol (GLD) were examined of their inactivation ability against scrapie-mo use prion protein (PrPSc) under various conditions of chemical concentratio n, incubation time, and temperature. Among these chemicals, GLD worked most effectively and degraded PrP into small fragments. As a result of the bioa ssay, treatment with 3% GLD for 5 hr and 5% GLD for 2, 5 hr or 12 hr at roo m temperature prolonged the mean incubation time by 44, 30, 110 and 73 days , respectively. From dose-incubation time standard curve, the decrease in i nfectivity titers were estimated as 10(3) or more. Therefore, degradation o f PrPSc by GLD decreased the scrapie infectivity. It is also suggested that pH and salt concentrations influence the effect of GLD. Although further s tudy is necessary to determine the optimal condition, GLD may be a potentia l prion disinfectant.