ArticlePLoS pathogens2022
Cryo-EM of prion strains from the same genotype of host identifies conformational determinants.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 55 citations in OpenAlex.
- Life at the interface: Byron Caughey's search for prion disease inhibitors through chemistry, structure, and cell physiology.Acta neuropathologica · 2026Review
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- The protein disulfide isomerase P4HB/PDIA1 modulates cellular and misfolded forms of the prion protein.PLoS pathogens · 2026Article
- The amyloid packing difference: A pairwise comparison metric for amyloid structures.Structure (London, England : 1993) · 2026Article
- Prion propagation is controlled by discrete structural regions of PrP rather than overall stability.The Journal of biological chemistry · 2026Article
- Generation of Infectious Prions Amenable to Site-Specific Click Chemistry.ACS chemical biology · 2026Article
- D178N prion protein mutation endows RML prions with new strain properties that do not mimic human genetic prion diseases.Acta neuropathologica · 2026Article
- Mutant knock-in mice display enhanced susceptibility to pure prion protein fibrils.The Journal of general virology · 2026Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties.Acta neuropathologica communications · 2025Article
- Review
- Evidence of a novel α-synuclein strain isolated from a Parkinson's disease with dementia patient sample.Acta neuropathologica communications · 2025Article
- Conservation of strain properties of bank vole-adapted chronic wasting disease in the absence of glycosylation and membrane anchoring.Neurobiology of disease · 2025Article
- Prion diseases: Lessons from historical outbreaks and potential emerging ones.Protein science : a publication of the Protein Society · 2025Review
- The Evolution of Experimental Rodent Models for Prion Diseases.Journal of neurochemistry · 2025Review
- Breaking the Mould: How the First Structure of a Deer Prion Suggests the Framework for Interspecies Strain Diversity and Transmission Barriers.Journal of neurochemistry · 2025Review
- Limitations and Applications of Rodent Models in Tauopathy and Synucleinopathy Research.Journal of neurochemistry · 2025Review
- Early Alzheimer's Disease with frequent neuritic plaques harbors neocortical tau seeds distinct from primary age-related tauopathy.Nature communications · 2025Article
- Chaperone-mediated disaggregation of infectious prions releases particles that seed new prion formation in a strain-specific manner.The Journal of biological chemistry · 2025Article
- Cofactors facilitate bona fide prion misfolding in vitro but are not necessary for the infectivity of recombinant murine prions.PLoS pathogens · 2025Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Prion strains in a given type of mammalian host are distinguished by differences in clinical presentation, neuropathological lesions, survival time, and characteristics of the infecting prion protein (PrP) assemblies. Near-atomic structures of prions from two host species with different PrP sequences have been determined but comparisons of distinct prion strains of the same amino acid sequence are needed to identify purely conformational determinants of prion strain characteristics. Here we report a 3.2 Å resolution cryogenic electron microscopy-based structure of the 22L prion strain purified from the brains of mice engineered to express only PrP lacking glycophosphatidylinositol anchors [anchorless (a) 22L]. Comparison of this near-atomic structure to our recently determined structure of the aRML strain propagated in the same inbred mouse reveals that these two mouse prion strains have distinct conformational templates for growth via incorporation of PrP molecules of the same sequence. Both a22L and aRML are assembled as stacks of PrP molecules forming parallel in-register intermolecular β-sheets and intervening loops, with single monomers spanning the ordered fibril core. Each monomer shares an N-terminal steric zipper, three major arches, and an overall V-shape, but the details of these and other conformational features differ markedly. Thus, variations in shared conformational motifs within a parallel in-register β-stack fibril architecture provide a structural basis for prion strain differentiation within a single host genotype.
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