Chemical Inactivation of Prions Is Altered by Binding to the Soil Mineral Montmorillonite.

Environmental routes of transmission contribute to the spread of the prion diseases chronic wasting disease of deer and elk and scrapie of sheep and goats. Prions can persist in soils and other environmental matrices and remain infectious for years. Prions bind avidly to the common soil mineral montmorillonite, and such binding can dramatically increase oral disease transmission.

Peroxymonosulfate Rapidly Inactivates the Disease-Associated Prion Protein.

Prions, the etiological agents in transmissible spongiform encephalopathies, exhibit remarkable resistance to most methods of inactivation that are effective against conventional pathogens. Prions are composed of pathogenic conformers of the prion protein (PrP(TSE)). Some prion diseases are transmitted, in part, through environmental routes.

Fate of prions in soil: a review.

Prions are the etiological agents of transmissible spongiform encephalopathies (TSSEs), a class of fatal neurodegenerative diseases affecting humans and other mammals. The pathogenic prion protein is a misfolded form of the host-encoded prion protein and represents the predominant, if not sole, component of the infectious agent. Environmental routes of TSE transmission areimplicated in epizootics of sheep scrapie and chronic wasting disease (CWD) of deer, elk, and moose.