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Abstract
Prions are the protein-based infectious agents responsible for prion diseases. Environmental prion contamination has been implicated in disease transmission. Here, we analyzed the binding and retention of infectious prion protein (PrP(Sc)) to plants. Small quantities of PrP(Sc) contained in diluted brain homogenate or in excretory materials (urine and feces) can bind to wheat grass roots and leaves. Wild-type hamsters were efficiently infected by ingestion of prion-contaminated plants. The prion-plant interaction occurs with prions from diverse origins, including chronic wasting disease. Furthermore, leaves contaminated by spraying with a prion-containing preparation retained PrP(Sc) for several weeks in the living plant. Finally, plants can uptake prions from contaminated soil and transport them to aerial parts of the plant (stem and leaves). These findings demonstrate that plants can efficiently bind infectious prions and act as carriers of infectivity, suggesting a possible role of environmental prion contamination in the horizontal transmission of the disease.
Highlights
Prions are the protein-based infectious agents responsible for prion diseases
To study whether plants can interact with prions, we exposed wheat grass roots and leaves to brain homogenate from hamsters that have succumbed to prion disease induced by experimental inoculation with the 263K prion strain
By comparing the detection of PrPSc-bound to plants (Fig. 1A) with an experiment in which the same dilutions of 263K brain homogenate were added directly to the tubes containing normal brain homogenate and an equivalent piece of leaves or roots (Fig. 1B), we can estimate that a high proportion of PrPSc present in the sample was attached to the plant tissue
Summary
Prions are the protein-based infectious agents responsible for prion diseases. Environmental prion contamination has been implicated in disease transmission. Plants can uptake prions from contaminated soil and transport them to aerial parts of the plant (stem and leaves) These findings demonstrate that plants can efficiently bind infectious prions and act as carriers of infectivity, suggesting a possible role of environmental prion contamination in the horizontal transmission of the disease. Some of the most prevalent and horizontally-transmissible animal TSEs, including scrapie and CWD, have implicated environmental contamination with prions as a putative mode of transmission (Mathiason et al, 2009; Gough and Maddison, 2010; Bartelt-Hunt and Bartz, 2013). Since the main natural hosts for animal TSEs (sheep, cattle and cervids) are herbivores, it is surprising that the interaction between prions and plants and the putative role of these organisms as carriers of prion infectivity has not been studied in detail. Our findings show that grass plants efficiently interact with prions, suggesting that they may play an important role in natural prion transmission, in wild animals
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