ArticleNeurobiology of disease2018
D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.
Article in Neurobiology of disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- Prion Protein Codon Implicated in Resistance in Dogs Detected in Non-Domesticated Members of Mammalia.Animals : an open access journal from MDPI · 2026Article
- First report of novel single-nucleotide polymorphisms and genetic characteristics in the open reading frame of the prion protein gene (Frontiers in veterinary science · 2026Article
- Novel polymorphisms and functional characterization of the prion protein gene in sparrows (Frontiers in veterinary science · 2026Article
- Phylogeny and Molecular Characterisation ofBrain sciences · 2025Article
- Distribution of chronic wasting disease (CWD) prions in tissues from experimentally exposed coyotes (Canis latrans).PloS one · 2025Article
- First Report of Polymorphisms and Genetic Characteristics ofAnimals : an open access journal from MDPI · 2024Article
- Conformational dynamics as an intrinsic determinant of prion protein misfolding and neurotoxicity.Neural regeneration research · 2024Article
- The First Genetic Characterization of theAnimals : an open access journal from MDPI · 2024Article
- The first report of single nucleotide polymorphisms in the open reading frame of the prion-like protein gene in rabbits.Frontiers in veterinary science · 2024Article
- Novel polymorphisms and genetic studies of the shadow of prion protein gene (Frontiers in veterinary science · 2024Article
- Novel polymorphisms in the prion protein gene (PRNP) and stability of the resultant prion protein in different horse breeds.Veterinary research · 2023Article
- First report of a novel polymorphism and genetic characteristics of the leporine prion protein (Frontiers in veterinary science · 2023Article
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- The first report of polymorphisms of the prion protein gene (Frontiers in veterinary science · 2023Article
- Probing the origin of prion protein misfolding via reconstruction of ancestral proteins.Protein science : a publication of the Protein Society · 2022Article
- New Drosophila models to uncover the intrinsic and extrinsic factors that mediate the toxicity of the human prion protein.Disease models & mechanisms · 2022Article
- Novel insertion/deletion polymorphisms and genetic features of the shadow of prion protein gene (Frontiers in veterinary science · 2022Article
- Huntington's disease: lessons from prion disorders.Journal of neurology · 2021Article
- Current and future applications of induced pluripotent stem cell-based models to study pathological proteins in neurodegenerative disorders.Molecular psychiatry · 2021Review
- The First Report of the Prion Protein Gene (Genes · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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.
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