Proteolytic inactivation of the bovine spongiform encephalopathy agent

被引：59

作者：

McLeod, AH

Murdoch, H

Dickinson, J

Dennis, MJ

Hall, GA

Buswell, CM

Carr, J

Taylor, DM

Sutton, JM

Raven, NDH

机构：

[1] Hlth Protect Agcy, Salisbury SP4 0JG, Wilts, England

[2] Sedecon 2000, Edinburgh EH13 9DX, Midlothian, Scotland

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 317卷 / 04期

关键词：

prion; transmissible spongiform encephalopathy; Creutzfeldt-Jakob disease; protease; thermophile; decontamination; surgical instruments; meat rendering;

D O I：

10.1016/j.bbrc.2004.03.168

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Thermostable proteases have been investigated for their ability to provide a novel biological solution to decontamination of prion agents responsible for transmissible spongiform encephalopathies (TSEs). Proteases were identified that digested total mouse brain homogenate (MBH) protein from uninfected mice. These proteases were then evaluated for digestion of BSE (301 V) infectious MBH over a range of pH and temperatures, screened for loss of anti-prion antibody 6H4 immunoreactivity and protease-treated infectious MBH assessed in mouse bioassay using VM mice. Despite a number of proteases eliminating all 61-14-immunoreactive material, only the subtilisin-enzyme Properase showed a significant extension in incubation period in mouse bioassays following a 30-min incubation at 60 degreesC and pH 12. These results demonstrate the potential of the method to provide a practical solution to the problems of TSE contamination of surgical instruments and highlight the inadequacy of using Western blot for assessment of decontamination/inactivation of TSE agents. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：1165 / 1170

页数：6

共 28 条

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