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Pathogenic prion protein is degraded by a manganese oxide mineral found in soils

Journal of General Virology

By:
, , , ,
DOI: 10.1099/vir.0.003251-0

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Abstract

Prions, the aetiological agents of transmissible spongiform encephalopathies, exhibit extreme resistance to degradation. Soil can retain prion infectivity in the environment for years. Reactive soil components may, however, contribute to the inactivation of prions in soil. Members of the birnessite family of manganese oxides (MnO2) rank among the strongest natural oxidants in soils. Here, we report the abiotic degradation of pathogenic prion protein (PrPTSE) by a synthetic analogue of naturally occurring birnessite minerals. Aqueous MnO2 suspensions degraded the PrPTSE as evidenced by decreased immunoreactivity and diminished ability to seed protein misfolding cyclic amplification reactions. Birnessite-mediated PrPTSE degradation increased as a solution's pH decreased, consistent with the pH-dependence of the redox potential of MnO2. Exposure to 5.6 mg MnO2 ml-1 (PrPTSE:MnO2=1 : 110) decreased PrPTSE levels by ???4 orders of magnitude. Manganese oxides may contribute to prion degradation in soil environments rich in these minerals. ?? 2009 SGM.

Additional Publication Details

Publication type:
Article
Publication Subtype:
Journal Article
Title:
Pathogenic prion protein is degraded by a manganese oxide mineral found in soils
Series title:
Journal of General Virology
DOI:
10.1099/vir.0.003251-0
Volume
90
Issue:
1
Year Published:
2009
Language:
English
Larger Work Type:
Article
Larger Work Subtype:
Journal Article
First page:
275
Last page:
280
Number of Pages:
6