ArticlePLoS pathogens2019
Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Optimizing plasma-derived small extracellular vesicle purification to enhance downstream applications.iScience · 2026Article
- Exploring and Targeting the Connection of Iron and Copper Homeostasis to Neurodegenerative Diseases.MedComm · 2026Review
- The octapeptide repeats of prion protein play critical roles in the pathogenesis of prion diseases.Acta neuropathologica communications · 2026Article
- Novel Prion Protein Gene (bioRxiv : the preprint server for biology · 2026Article
- Identification and initial characterization of novel prion protein gene (Frontiers in veterinary science · 2026Article
- Exploring immunotherapeutic strategies for neurodegenerative diseases: a focus on Huntington's disease and Prion diseases.Acta pharmacologica Sinica · 2025Review
- Inhibition of amyloid formation of prion fragment (106-128) by polyphenolic compounds.Biochimica et biophysica acta. General subjects · 2025Article
- Investigating the In Vivo Effects of Anti-Prion Protein Nanobodies on Prion Disease with AAV Vector.Pathogens (Basel, Switzerland) · 2025Article
- Unfolding Mechanism and Fibril Formation Propensity of Human Prion Protein in the Presence of Molecular Crowding Agents.International journal of molecular sciences · 2024Article
- Differential expression of cellular prion protein (PrPJournal of neurovirology · 2024Article
- Single-domain antibodies and aptamers drive new opportunities for neurodegenerative disease research.Frontiers in immunology · 2024Review
- Protein-protein interaction site prediction by model ensembling with hybrid feature and self-attention.BMC bioinformatics · 2023Article
- Copper coordination modulates prion conversion and infectivity in mammalian prion proteins.Prion · 2023Review
- Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Inducing prion protein shedding as a neuroprotective and regenerative approach in pathological conditions of the brain: from theory to facts.Neural regeneration research · 2023Review
- Advanced Situation with Recombinant Toxins: Diversity, Production and Application Purposes.International journal of molecular sciences · 2023Review
- Recognition Mechanisms between a Nanobody and Disordered Epitopes of the Human Prion Protein: An Integrative Molecular Dynamics Study.Journal of chemical information and modeling · 2023Article
- Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein.Chemical science · 2022Article
- Prion Protein: The Molecule of Many Forms and Faces.International journal of molecular sciences · 2022Review
- Applications of nanobodies in brain diseases.Frontiers in immunology · 2022Review
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Authors and funding
11 authors.
Funding
Abstract
Prion or PrPSc is the proteinaceous infectious agent causing prion diseases in various mammalian species. Despite decades of research, the structural basis for PrPSc formation and prion infectivity remains elusive. To understand the role of the hydrophobic region in forming infectious prion at the molecular level, we report X-ray crystal structures of mouse (Mo) prion protein (PrP) (residues 89-230) in complex with a nanobody (Nb484). Using the recombinant prion propagation system, we show that the binding of Nb484 to the hydrophobic region of MoPrP efficiently inhibits the propagation of proteinase K resistant PrPSc and prion infectivity. In addition, when added to cultured mouse brain slices in high concentrations, Nb484 exhibits no neurotoxicity, which is drastically different from other neurotoxic anti-PrP antibodies, suggesting that the Nb484 can be a potential therapeutic agent against prion disease. In summary, our data provides the first structure-function evidence supporting a crucial role of the hydrophobic region of PrP in forming an infectious prion.
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