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Frontiers in cellular neuroscience2020; 14; 254; doi: 10.3389/fncel.2020.00254

Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype – Morphotype – Phenotype Code for the Prion Protein.

Abstract: Prion diseases are a group of neurodegenerative diseases endemic in humans and several ruminants caused by the misfolding of native prion protein (PrP) into pathological conformations. Experimental work and the mad-cow epidemic of the 1980s exposed a wide spectrum of animal susceptibility to prion diseases, including a few highly resistant animals: horses, rabbits, pigs, and dogs/canids. The variable susceptibility to disease offers a unique opportunity to uncover the mechanisms governing PrP misfolding, neurotoxicity, and transmission. Previous work indicates that PrP-intrinsic differences (sequence) are the main contributors to disease susceptibility. Several residues have been cited as critical for encoding PrP conformational stability in prion-resistant animals, including D/E159 in dog, S167 in horse, and S174 in rabbit and pig PrP (all according to human numbering). These amino acids alter PrP properties in a variety of assays, but we still do not clearly understand the structural correlates of PrP toxicity. Additional insight can be extracted from comparative structural studies, followed by molecular dynamics simulations of selected mutations, and testing in manipulable animal models. Our working hypothesis is that protective amino acids generate more compact and stable structures in a C-terminal subdomain of the PrP globular domain. We will explore this idea in this review and identify subdomains within the globular domain that may hold the key to unravel how conformational stability and disease susceptibility are encoded in PrP.
Copyright © 2020 Myers, Cembran and Fernandez-Funez.
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Publication Date: 2020-08-18 PubMed ID: 33013324PubMed Central: PMC7461849DOI: 10.3389/fncel.2020.00254Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article explores prion diseases and why certain animals like horses, rabbits, pigs, and dogs tend to be more resistant to them. The researchers hypothesize that specific amino acids may contribute to a certain level of protection against these diseases and aim to understand the relationship between the prion protein structure, and disease susceptibility.

Understanding Prion Diseases

  • The study is focused on prion diseases, which are a collection of diseases caused by the abnormal folding of the prion protein (PrP) in the brain, leading to brain damage. These diseases are endemic in humans and various ruminants (cows, sheep, etc.).
  • The article explores the varying susceptibility to prion diseases across different animal species. Some species are highly resistant to these diseases, including horses, rabbits, pigs, and dogs.

Intrinsic Differences in PrP and Disease Susceptibility

  • Previous research by the team indicates that the critical factor contributing to an organism’s susceptibility to prion diseases is intrinsic differences in the prion protein itself.
  • Particular amino acids in the prion protein are thought to shape its overall stability, which has implications for an organism’s predisposition to these neurodegenerative diseases.
  • For instance, the presence of the amino acids D/E159 in dogs, S167 in horses, and S174 in rabbits and pigs, stirs a change in prion protein properties, making these animals more resistant to prion diseases.

Advanced Research: Unraveling the PrP Structure-Disease Link

  • However, it isn’t clear yet how the structural properties of the prion protein correspond to its potential for toxicity.
  • To address this gap, the researchers propose a comprehensive research approach that combines comparative structural studies, simulations of selected mutations using molecular dynamics, and testing on animal models that are easy to manipulate genetically.
  • The researchers hypothesize that certain protective amino acids change the structure of a subset of the prion protein, making it more compact and stable.
  • They aim to explore this idea further and identify specific regions within this protein structure that could elucidate how prion protein stability interlinks with disease susceptibility.

Cite This Article

APA
Myers R, Cembran A, Fernandez-Funez P. (2020). Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype – Morphotype – Phenotype Code for the Prion Protein. Front Cell Neurosci, 14, 254. https://doi.org/10.3389/fncel.2020.00254

Publication

Frontiers in cellular neuroscience
ISSN: 1662-5102
NlmUniqueID: 101477935
Country: Switzerland
Language: English
Volume: 14
Pages: 254
PII: 254

Researcher Affiliations

Myers, Ryan
  • Department of Biomedical Sciences, University of Minnesota Medical School, Duluth, MN, United States.
Cembran, Alessandro
  • Department of Chemistry and Biochemistry, University of Minnesota Duluth, Duluth, MN, United States.
Fernandez-Funez, Pedro
  • Department of Biomedical Sciences, University of Minnesota Medical School, Duluth, MN, United States.

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Citations

This article has been cited 10 times.
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