ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2014
Prion transmission prevented by modifying the β2-α2 loop structure of host PrPC.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 78 citations in OpenAlex.
- Prion propagation is controlled by discrete structural regions of PrP rather than overall stability.The Journal of biological chemistry · 2026Article
- Limited transmission of cervid prions to nonhuman primates provides insights into the zoonotic potential of chronic wasting disease.Science advances · 2026Article
- Bovine Spongiform Encephalopathy: An Integrated Review of Prion Mechanisms, Neuroanatomy, and Control.Veterinary sciences · 2026Review
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Strain-Dependent Susceptibility to Prion Infection Encoded by Arg171 and Lys176 Sheep Prion Protein Polymorphic Variants.The Journal of infectious diseases · 2025Article
- Exploring immunotherapeutic strategies for neurodegenerative diseases: a focus on Huntington's disease and Prion diseases.Acta pharmacologica Sinica · 2025Review
- Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer.Acta neuropathologica · 2024Article
- Norwegian moose CWD induces clinical disease and neuroinvasion in gene-targeted mice expressing cervid S138N prion protein.PLoS pathogens · 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
- Genetic modulation of CWD prion propagation in cervid PrP Drosophila.The Biochemical journal · 2023Article
- A structural basis for prion strain diversity.Nature chemical biology · 2023Article
- The Zoonotic Potential of Chronic Wasting Disease-A Review.Foods (Basel, Switzerland) · 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
- The first report of polymorphisms of the prion protein gene (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
- Chronic wasting disease: a cervid prion infection looming to spillover.Veterinary research · 2021Review
- The polyphenolic phytoalexin polydatin inhibits amyloid aggregation of recombinant human prion protein.RSC advances · 2021Article
- MetNeuropathology and applied neurobiology · 2021Article
- Cervid Prion Protein Polymorphisms: Role in Chronic Wasting Disease Pathogenesis.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
Abstract
Zoonotic prion transmission was reported after the bovine spongiform encephalopathy (BSE) epidemic, when >200 cases of prion disease in humans were diagnosed as variant Creutzfeldt-Jakob disease. Assessing the risk of cross-species prion transmission remains challenging. We and others have studied how specific amino acid residue differences between species impact prion conversion and have found that the β2-α2 loop region of the mouse prion protein (residues 165-175) markedly influences infection by sheep scrapie, BSE, mouse-adapted scrapie, deer chronic wasting disease, and hamster-adapted scrapie prions. The tyrosine residue at position 169 is strictly conserved among mammals and an aromatic side chain in this position is essential to maintain a 310-helical turn in the β2-α2 loop. Here we examined the impact of the Y169G substitution together with the previously described S170N, N174T "rigid loop" substitutions on cross-species prion transmission in vivo and in vitro. We found that transgenic mice expressing mouse PrP containing the triple-amino acid substitution completely resisted infection with two strains of mouse prions and with deer chronic wasting disease prions. These studies indicate that Y169 is important for prion formation, and they provide a strong indication that variation of the β2-α2 loop structure can modulate interspecies prion transmission.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.