ArticlePLoS pathogens2025
Cofactors facilitate bona fide prion misfolding in vitro but are not necessary for the infectivity of recombinant murine prions.
Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Concise Total Synthesis and Pharmacological Evaluation of Procerones A and B.ACS pharmacology & translational science · 2026Article
- Leveraging the dominant-negative effect of the kuru-protective G127V prion protein variant as a novel therapeutic strategy.Neurobiology of disease · 2026Article
- Rapid generation of prion disease models using AAV-delivered PrP variants in knockout mice.Brain pathology (Zurich, Switzerland) · 2026Article
- The L108I polymorphism in mouse prion protein drives spontaneous disease and enhances transmission of atypical and classical prion strains.Brain pathology (Zurich, Switzerland) · 2026Article
- The axonal transport velocity of prions is independent of prion formation.PLoS pathogens · 2026Article
- Leveraging the dominant-negative effect of the kuru-protective G127V prion protein variant as a novel therapeutic strategy.bioRxiv : the preprint server for biology · 2026Article
- Mutant knock-in mice display enhanced susceptibility to pure prion protein fibrils.The Journal of general virology · 2026Article
- Overexpression of bank vole PrP(I109) in mice induces a spontaneous atypical prion disease with sex-dependent onset, early NfL elevation, and universal prion strain permissiveness.Acta neuropathologica communications · 2026Article
- Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties.Acta neuropathologica communications · 2025Article
- Effect of primary structural variation on cervid prion protein in flexibility, stability, and spontaneous misfolding propensity.Neurobiology of disease · 2025Article
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17 authors.
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Abstract
Prion diseases, particularly sporadic cases, pose a challenge due to their complex nature and heterogeneity. The underlying mechanism of the spontaneous conversion from PrPC to PrPSc, the hallmark of prion diseases, remains elusive. To shed light on this process and the involvement of cofactors, we have developed an in vitro system that faithfully mimics spontaneous prion misfolding using minimal components. By employing this PMSA methodology and introducing an isoleucine residue at position 108 in mouse PrP, we successfully generated recombinant murine prion strains with distinct biochemical and biological properties. Our study aimed to explore the influence of a polyanionic cofactor in modulating strain selection and infectivity in de novo-generated synthetic prions. These results not only validate PMSA as a robust method for generating diverse bona fide recombinant prions but also emphasize the significance of cofactors in shaping specific prion conformers capable of crossing species barriers. Interestingly, once these conformers are established, our findings suggest that cofactors are not necessary for their infectivity. This research provides valuable insights into the propagation and maintenance of the pathobiological features of cross-species transmissible recombinant murine prion and highlights the intricate interplay between cofactors and prion strain characteristics.
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