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Home / Equine Research Bank / Neurobiol Dis / D159 and S167 are protective residues in the prion protein f...
Neurobiology of disease2018; 119; 1-12; doi: 10.1016/j.nbd.2018.07.011

D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.

Abstract: Prion diseases are fatal neurodegenerative diseases caused by misfolding of the prion protein (PrP). These conditions affect humans and animals, including endemic forms in sheep and deer. Bovine, rodents, and many zoo mammals also developed prion diseases during the "mad-cow" epidemic in the 1980's. Interestingly, rabbits, horses, and dogs show unusual resistance to prion diseases, suggesting that specific sequence changes in the corresponding endogenous PrP prevents the accumulation of pathogenic conformations. In vitro misfolding assays and structural studies have identified S174, S167, and D159 as the key residues mediating the stability of rabbit, horse, and dog PrP, respectively. Here, we expressed the WT forms of rabbit, horse, and dog PrP in transgenic Drosophila and found that none of them is toxic. Replacing these key residues with the corresponding amino acids in hamster PrP showed that mutant horse (S167D) and dog (D159N) PrP are highly toxic, whereas mutant rabbit (S174 N) PrP is not. These results confirm the impact of S167 and D159 in local and long-range structural features in the globular domain of PrP that increase its stability, while suggesting the role of additional residues in the stability of rabbit PrP. Identifying these protective amino acids and the structural features that stabilize PrP can contribute to advance the field towards the development of therapies that halt or reverse the devastating effects of prion diseases.
Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.
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Publication Date: 2018-07-24 PubMed ID: 30010001PubMed Central: PMC6139044DOI: 10.1016/j.nbd.2018.07.011Google 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.

This research article discusses the animal protein (PrP) found in rabbits, horses, and dogs that make them resistant to prion diseases, specifically, the research identifies the key residues that stabilise these proteins. They found that the replacement of these residues can result in toxicity, confirming their protective role against Prion diseases.

Prion Diseases and Prion Protein

  • Prion diseases are fatal neurodegenerative conditions caused by the misfolding of the prion protein (PrP). These diseases impact both humans and animals, with endemic cases being reported among sheep and deer populations.
  • During the “mad-cow” epidemic in the 1980s, PrP diseases were also observed in bovines, rodents, and multiple species of zoo animals.

The Role of PrP in Animals Resistant to Prion Diseases

  • Certain animals, such as rabbits, horses, and dogs, demonstrate unusual resistance to PrP diseases. Researchers suggest that this is due to specific sequence alterations in the respective endogenous PrP of these animals, which avoid the build-up of pathogenic conformations.
  • Misfolding assays and structural studies were used to identify residues S174, S167, and D159 as key roles in maintaining the stability of rabbit, horse, and dog PrP respectively.
  • In this study, they expressed the wildtype forms of rabbit, horse, and dog PrP in transgenic Drosophila and noted that none of these lead to toxicity.

Replacing Key Residues

  • Following the replacement of these key residues with similar amino acids found in hamster PrP, results showed that mutant horse (S167D) and dog (D159N) PrP became highly toxic.
  • By contrast, mutant rabbit (S174 N) PrP did not display toxicity, implying that in addition to S174, other residues may also play a role in stabilising rabbit PrP.

Impact on Prion Disease Therapies

  • The discovery of these protective residues and the structural features that maintain PrP stability provides valuable insights that could facilitate the engineered development of therapies to either halt or reverse the damaging effects of Prion diseases.

Cite This Article

APA
Sanchez-Garcia J, Fernandez-Funez P. (2018). D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals. Neurobiol Dis, 119, 1-12. https://doi.org/10.1016/j.nbd.2018.07.011

Publication

Neurobiology of disease
ISSN: 1095-953X
NlmUniqueID: 9500169
Country: United States
Language: English
Volume: 119
Pages: 1-12
PII: S0969-9961(18)30248-1

Researcher Affiliations

Sanchez-Garcia, Jonatan
  • Department of Biomedical Sciences, University of Minnesota Medical School, Duluth Campus, Duluth, MN 55812, USA.
Fernandez-Funez, Pedro
  • Department of Biomedical Sciences, University of Minnesota Medical School, Duluth Campus, Duluth, MN 55812, USA. Electronic address: pfernand@d.umn.edu.

MeSH Terms

  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified
  • Cricetinae
  • Dogs
  • Drosophila
  • Female
  • Horses
  • Humans
  • Locomotion / physiology
  • Mice
  • Prion Diseases / genetics
  • Prion Diseases / physiopathology
  • Prion Diseases / prevention & control
  • Prion Proteins / chemistry
  • Prion Proteins / genetics
  • Protein Structure, Secondary
  • Rabbits
  • Species Specificity

Grant Funding

  • DP2 OD002721 / NIH HHS
  • R21 NS096627 / NINDS NIH HHS

Conflict of Interest Statement

Competing Interests. The authors declare that no competing interests exist.

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Citations

This article has been cited 26 times.
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