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Review
. 2024 Feb 2;13(2):138.
doi: 10.3390/pathogens13020138.

Chronic Wasting Disease: State of the Science

Jason C Bartz  1 , Rebeca Benavente  2 , Byron Caughey  3 , Sonja Christensen  4 , Allen Herbst  5 , Edward A Hoover  6 , Candace K Mathiason  6 , Debbie McKenzie  7 , Rodrigo Morales  2   8 , Marc D Schwabenlander  9 , Daniel P Walsh  10 , The Nc North American Interdisciplinary Chronic Wasting Disease Research Consortium Members
Affiliations
Review

Chronic Wasting Disease: State of the Science

Jason C Bartz et al. Pathogens. .

Abstract

Chronic wasting disease (CWD) is a prion disease affecting cervid species, both free-ranging and captive populations. As the geographic range continues to expand and disease prevalence continues to increase, CWD will have an impact on cervid populations, local economies, and ecosystem health. Mitigation of this "wicked" disease will require input from many different stakeholders including hunters, landowners, research biologists, wildlife managers, and others, working together. The NC1209 (North American interdisciplinary chronic wasting disease research consortium) is composed of scientists from different disciplines involved with investigating and managing CWD. Leveraging this broad breadth of expertise, the Consortium has created a state-of-the-science review of five key aspects of CWD, including current diagnostic capabilities for detecting prions, requirements for validating these diagnostics, the role of environmental transmission in CWD dynamics, and potential zoonotic risks associated with CWD. The goal of this review is to increase stakeholders', managers', and decision-makers' understanding of this disease informed by current scientific knowledge.

Keywords: PMCA; RT-QuIC; cervids; environmental prions; interspecies transmission; prion disease; zoonosis.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
A graphical representation of the PMCA methods and samples where CWD has been detected. Figure generated by BioRender.
Figure 2
Figure 2
Schematic of the RT-QuIC assay readout. Annotated are time-dependent threshold crossings, or lack thereof, with the fluorescent readings taken at each time point illustrated by the colored asterisks where red, orange and blue asterisks represent readings of positive samples and green asterisks represent reading of the negative sample.
Figure 3
Figure 3
CWD prions are shed by infected hosts via urine, feces, and saliva. These prions are maintained in the environment by binding to vegetation and/or soil. Ingestion of soil/vegetation results in further transmission. Black arrows depict CWD prion cycling between hosts and the environment. White arrow depicts CWD prion migration through soils. Figure generated by BioRender.
Figure 4
Figure 4
The infection cycle indicates sources of CWD for interspecies transmission.
See this image and copyright information in PMC

References

    1. Williams E.S., Young S. Chronic wasting disease of captive mule deer: A spongiform encephalopathy. J. Wildl. Dis. 1980;16:89–98. doi: 10.7589/0090-3558-16.1.89. - DOI - PubMed
    1. Deleault N.R., Harris B.T., Rees J.R., Supattapone S. Formation of native prions from minimal components in vitro. Proc. Natl. Acad. Sci. USA. 2007;104:9741–9746. doi: 10.1073/pnas.0702662104. - DOI - PMC - PubMed
    1. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science. 1982;216:136–144. doi: 10.1126/science.6801762. - DOI - PubMed
    1. Kraus A., Hoyt F., Schwartz C.L., Hansen B., Artikis E., Hughson A.G., Raymond G.J., Race B., Baron G.S., Caughey B. High-resolution structure and strain comparison of infectious mammalian prions. Mol. Cell. 2021;81:4540–4551.e4546. doi: 10.1016/j.molcel.2021.08.011. - DOI - PubMed
    1. Kocisko D.A., Come J.H., Priola S.A., Chesebro B., Raymond G.J., Lansbury P.T., Caughey B. Cell-free formation of protease-resistant prion protein. Nature. 1994;370:471–474. doi: 10.1038/370471a0. - DOI - PubMed