ArticleThe Journal of biological chemistry2010
Unique structural characteristics of the rabbit prion protein.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 106 citations in OpenAlex.
- Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Comparing Prion Proteins Across Species: Is Zebrafish a Useful Model?Molecular neurobiology · 2025Review
- First Report of Single Nucleotide Polymorphisms (SNPs) of the Leporine Shadow of Prion Protein Gene (Animals : an open access journal from MDPI · 2024Article
- Prion protein E219K polymorphism: from the discovery of the KANNO blood group to interventions for human prion disease.Frontiers in neurology · 2024Review
- 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
- 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
- Structural consequences of sequence variation in mammalian prion β2α2 loop segments.Frontiers in neuroscience · 2022Article
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype - Morphotype - Phenotype Code for the Prion Protein.Frontiers in cellular neuroscience · 2020Review
- Detecting early stage structural changes in wild type, pathogenic and non-pathogenic prion variants using Markov state model.RSC advances · 2019Article
- D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.Neurobiology of disease · 2018Article
- Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease.Scientific reports · 2018Article
- Article
- Asparagine and glutamine ladders promote cross-species prion conversion.The Journal of biological chemistry · 2017Article
- Unraveling the key to the resistance of canids to prion diseases.PLoS pathogens · 2017Article
- Prion proteinProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interplay of buried histidine protonation and protein stability in prion misfolding.Scientific reports · 2017Article
- Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.PloS one · 2017Article
- Unique Properties of the Rabbit Prion Protein Oligomer.PloS one · 2016Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rabbits are one of the few mammalian species that appear to be resistant to transmissible spongiform encephalopathies due to the structural characteristics of the rabbit prion protein (RaPrP(C)) itself. Here, we determined the solution structures of the recombinant protein RaPrP(C)-(91-228) and its S173N variant and detected the backbone dynamics of their structured C-terminal domains-(121-228). In contrast to many other mammalian PrP(C)s, loop 165-172, which connects β-sheet-2 and α-helix-2, is well-defined in RaPrP(C). For the first time, order parameters S(2) are obtained for residues in this loop region, indicating that loop 165-172 of RaPrP(C) is highly ordered. Compared with the wild-type RaPrP(C), less hydrogen bonds form in the S173N variant. The NMR dynamics analysis reveals a distinct increase in the structural flexibility of loop 165-172 and helix-3 after the S173N substitution, implying that the S173N substitution disturbs the long range interaction of loop 165-172 with helix-3, which further leads to a marked decrease in the global conformational stability. Significantly, RaPrP(C) possesses a unique charge distribution, carrying a continuous area of positive charges on the surface, which is distinguished from other PrP(C)s. The S173N substitution causes visible changes of the charge distribution around the recognition sites for the hypothetical protein X. Our results suggest that the ordered loop 165-172 and its interaction with helix-3, together with the unique distribution of surface electrostatic potential, significantly contribute to the unique structural characteristics of RaPrP(C).
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