Can plants serve as a vector for prions causing chronic wasting disease?

Rasmussen, Jay; Gilroyed, Brandon H.; Reuter, Tim; Dudas, Sandor; Neumann, Norman F.; Balachandran, Aru; Kav, Nat N. V.; Graham, Catherine; Czub, Stefanie; McAllister, Tim A.

doi:10.4161/pri.27963

Cited by 16 publications

(10 citation statements)

References 34 publications

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“…5B), indicating that prions were uptaken from the soil and transported into the aerial parts of the plants, far from the soil. These results differ from a recent article reporting that infectious prions were not detectable in above the ground tissues of wheat plants exposed to CWD prions (Rasmussen et al, 2014). The lack of detection in this article is most likely due to the low sensitive techniques (western blots or ELISA) employed to analyze the presence of PrP Sc .…”

Section: Resultscontrasting

confidence: 99%

Grass Plants Bind, Retain, Uptake, and Transport Infectious Prions

Pritzkow¹,

Morales²,

Moda³

et al. 2015

Cell Reports

111

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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 (PrPSc) to plants. Small quantities of PrPSc 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 PrPSc 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.

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Section: Resultscontrasting

confidence: 99%

Grass Plants Bind, Retain, Uptake, and Transport Infectious Prions

Pritzkow¹,

Morales²,

Moda³

et al. 2015

Cell Reports

111

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“…Under environmental transmission, we assumed that food consumption was the major route of the disease spread through environmental contamination and that juveniles were less likely to be infected than adults because they eat less food that could be contaminated. Ingestion of infected soils, directly or indirectly, on plant material is most likely because current studies provide little evidence of the transport of CWD from roots to the stem and leaves of plants [ 22 ]. The low rate of infection of young is consistent with observed patterns of lower prevalence in fawns in general (e.g.…”

Section: Discussionmentioning

confidence: 99%

Chronic Wasting Disease: Transmission Mechanisms and the Possibility of Harvest Management

et al. 2016

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We develop a model of CWD management by nonselective deer harvest, currently the most feasible approach available for managing CWD in wild populations. We use the model to explore the effects of 6 common harvest strategies on disease prevalence and to identify potential optimal harvest policies for reducing disease prevalence without population collapse. The model includes 4 deer categories (juveniles, adult females, younger adult males, older adult males) that may be harvested at different rates, a food-based carrying capacity, which influences juvenile survival but not adult reproduction or survival, and seasonal force of infection terms for each deer category under differing frequency-dependent transmission dynamics resulting from environmental and direct contact mechanisms. Numerical experiments show that the interval of transmission coefficients β where the disease can be controlled is generally narrow and efficiency of a harvest policy to reduce disease prevalence depends crucially on the details of the disease transmission mechanism, in particular on the intensity of disease transmission to juveniles and the potential differences in the behavior of older and younger males that influence contact rates. Optimal harvest policy to minimize disease prevalence for each of the assumed transmission mechanisms is shown to depend on harvest intensity. Across mechanisms, a harvest that focuses on antlered deer, without distinguishing between age classes reduces disease prevalence most consistently, whereas distinguishing between young and older antlered deer produces higher uncertainty in the harvest effects on disease prevalence. Our results show that, despite uncertainties, a modelling approach can determine classes of harvest strategy that are most likely to be effective in combatting CWD.

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“…440 Pritzkow et al used protein misfolded cyclic amplification (PMCA) as a more sensitive detection method and transmitted hamster 263K PrP Sc to wheat grass roots via infected brain homogenate, excreta, contaminated soils and direct spray of PrP on areal parts. 441 The 263K PrP Sc were able to adsorb from the sources to the roots and travelled in the areal parts, which were further able to reproduce the infectivity in naïve hamster.…”

Section: Prions and Prion Diseasesmentioning

confidence: 99%

Implications of peptide assemblies in amyloid diseases

et al. 2017

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Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the quality of life of millions worldwide, with profound social and economic implications. Despite the significant differences in pathology – much of which are poorly understood – these diseases are commonly characterized by the presence of cross-β amyloid fibrils as well as the loss of neuronal or pancreatic β-cells. In this review, we document research progress on the molecular and mesoscopic self-assembly of amyloid-beta, alpha synuclein, human islet amyloid polypeptide and prions, the peptides and proteins associated with Alzheimer’s, Parkinson’s, type 2 diabetes and prions diseases. In addition, we discuss the toxicities of these amyloid proteins based on their self-assembly as well as their interactions with membranes, metal ions, small molecules and engineered nanoparticles. Through this presentation we show the remarkable similarities and differences in the structural transitions of the amyloid proteins through primary and secondary nucleation, the common evolution from disordered monomers to alpha-helices and then to β-sheets when the proteins encounter the cell membrane, and, the consensus (with a few exceptions) that off-pathway oligomers, rather than amyloid fibrils, are the toxic species regardless of the pathogenic protein sequence or physicochemical properties. In addition, we highlight the crucial role of molecular self-assembly in eliciting the biological and pathological consequences of the amyloid proteins within the context of their cellular environments and their spreading between cells and organs. Exploiting such structure-function-toxicity relationship may prove pivotal for the detection and mitigation of amyloid diseases.

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Can plants serve as a vector for prions causing chronic wasting disease?

Cited by 16 publications

References 34 publications

Grass Plants Bind, Retain, Uptake, and Transport Infectious Prions

Grass Plants Bind, Retain, Uptake, and Transport Infectious Prions

Chronic Wasting Disease: Transmission Mechanisms and the Possibility of Harvest Management

Implications of peptide assemblies in amyloid diseases

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