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ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Virus and Prion Research » Research » Publications at this Location » Publication #389366

Research Project: Elucidating the Pathobiology and Transmission of Transmissible Spongiform Encephalopathies

Location: Virus and Prion Research

Title: Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases

Author
item LAMBERT, ZOE - Oak Ridge Institute For Science And Education (ORISE)
item Greenlee, Justin
item Cassmann, Eric
item WEST GREENLEE, HEATHER - Iowa State University

Submitted to: Viruses
Publication Type: Review Article
Publication Acceptance Date: 12/2/2021
Publication Date: 12/7/2021
Citation: Lambert, Z., Greenlee, J.J., Cassmann, E.D., West Greenlee, H.M. 2021. Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases. Viruses. 13(12). https://doi.org/10.3390/v13122453.
DOI: https://doi.org/10.3390/v13122453

Interpretive Summary:

Technical Abstract: Prion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are a group of protein misfolding diseases that invariably cause death. TSEs occur when the endogenous cellular prion protein (PrPC) misfolds to form the pathological prion protein (PrPSc), which templates further conversion of PrPC to PrPSc. Interestingly, the different strains of prion diseases are thought to arise from the differential misfolding of the prion protein. Further, different strains of prion diseases accumulate PrPSc differentially in the tissues of natural hosts. This differential ac-cumulation occurs in the retinal ganglion cells, cerebellar cortex and white matter, and plexuses of the enteric nervous system in cattle with bovine spongiform encephalopathy, sheep and goats with scrapie, cervids with chronic wasting disease, and humans with prion diseases. By characterizing TSEs in their natural host, scientists can better understand the pathogenesis of different prion strains. This information is valuable in the pursuit of evaluating and discovering potential biomarkers and therapeutics for prion diseases. In this review, we summarize the differential accumulation of the misfolded prion protein in the natural hosts of these TSEs.