Prions adhere to soil minerals and remain infectious.

An unidentified environmental reservoir of infectivity contributes to the natural transmission of prion diseases (transmissible spongiform encephalopathies [TSEs]) in sheep, deer, and elk. Prion infectivity may enter soil environments via shedding from diseased animals and decomposition of infected...

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Format: Article
Language:English
Published: Public Library of Science (PLoS) 2006-04-01
Series:PLoS Pathogens
Online Access:http://dx.doi.org/10.1371/journal.ppat.0020032
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collection DOAJ
description An unidentified environmental reservoir of infectivity contributes to the natural transmission of prion diseases (transmissible spongiform encephalopathies [TSEs]) in sheep, deer, and elk. Prion infectivity may enter soil environments via shedding from diseased animals and decomposition of infected carcasses. Burial of TSE-infected cattle, sheep, and deer as a means of disposal has resulted in unintentional introduction of prions into subsurface environments. We examined the potential for soil to serve as a TSE reservoir by studying the interaction of the disease-associated prion protein (PrP(Sc)) with common soil minerals. In this study, we demonstrated substantial PrP(Sc) adsorption to two clay minerals, quartz, and four whole soil samples. We quantified the PrP(Sc)-binding capacities of each mineral. Furthermore, we observed that PrP(Sc) desorbed from montmorillonite clay was cleaved at an N-terminal site and the interaction between PrP(Sc) and Mte was strong, making desorption of the protein difficult. Despite cleavage and avid binding, PrP(Sc) bound to Mte remained infectious. Results from our study suggest that PrP(Sc) released into soil environments may be preserved in a bioavailable form, perpetuating prion disease epizootics and exposing other species to the infectious agent.
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spelling doaj.art-a1bcdca3f89a408a9a8a398e9266a2892022-12-22T03:06:43ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742006-04-0124e32Prions adhere to soil minerals and remain infectious.An unidentified environmental reservoir of infectivity contributes to the natural transmission of prion diseases (transmissible spongiform encephalopathies [TSEs]) in sheep, deer, and elk. Prion infectivity may enter soil environments via shedding from diseased animals and decomposition of infected carcasses. Burial of TSE-infected cattle, sheep, and deer as a means of disposal has resulted in unintentional introduction of prions into subsurface environments. We examined the potential for soil to serve as a TSE reservoir by studying the interaction of the disease-associated prion protein (PrP(Sc)) with common soil minerals. In this study, we demonstrated substantial PrP(Sc) adsorption to two clay minerals, quartz, and four whole soil samples. We quantified the PrP(Sc)-binding capacities of each mineral. Furthermore, we observed that PrP(Sc) desorbed from montmorillonite clay was cleaved at an N-terminal site and the interaction between PrP(Sc) and Mte was strong, making desorption of the protein difficult. Despite cleavage and avid binding, PrP(Sc) bound to Mte remained infectious. Results from our study suggest that PrP(Sc) released into soil environments may be preserved in a bioavailable form, perpetuating prion disease epizootics and exposing other species to the infectious agent.http://dx.doi.org/10.1371/journal.ppat.0020032
spellingShingle Prions adhere to soil minerals and remain infectious.
PLoS Pathogens
title Prions adhere to soil minerals and remain infectious.
title_full Prions adhere to soil minerals and remain infectious.
title_fullStr Prions adhere to soil minerals and remain infectious.
title_full_unstemmed Prions adhere to soil minerals and remain infectious.
title_short Prions adhere to soil minerals and remain infectious.
title_sort prions adhere to soil minerals and remain infectious
url http://dx.doi.org/10.1371/journal.ppat.0020032