ArticleProceedings of the National Academy of Sciences of the United States of America2011
Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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, 59 citations in OpenAlex.
- Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C).PLoS pathogens · 2012Trial
- PMCA screening of retropharyngeal lymph nodes in white-tailed deer and comparisons with ELISA and IHC.Scientific reports · 2023Article
- Structurally distinct external solvent-exposed domains drive replication of major human prions.PLoS pathogens · 2021Article
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Article
- In vitro Modeling of Prion Strain Tropism.Viruses · 2019Review
- Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein.Acta neuropathologica communications · 2018Article
- Artificial strain of human prions created in vitro.Nature communications · 2018Article
- Prion replication environment defines the fate of prion strain adaptation.PLoS pathogens · 2018Article
- Experimental transfusion of variant CJD-infected blood reveals previously uncharacterised prion disorder in mice and macaque.Nature communications · 2017Article
- PrP P102L and Nearby Lysine Mutations Promote SpontaneousJournal of virology · 2017Article
- Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.PLoS pathogens · 2017Article
- Sialylation Controls Prion FateThe Journal of biological chemistry · 2017Article
- Infectious prions and proteinopathies.Prion · 2017Article
- Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Scientific reports · 2016Article
- Peroxymonosulfate Rapidly Inactivates the Disease-Associated Prion Protein.Environmental science & technology · 2016Article
- Article
- Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion protein.Journal of virology · 2015Article
- Shedding light on prion disease.Prion · 2015Article
- Article
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Abstract
Prions are unconventional infectious agents that cause transmissible spongiform encephalopathy (TSE) diseases, or prion diseases. The biochemical nature of the prion infectious agent remains unclear. Previously, using a protein misfolding cyclic amplification (PMCA) reaction, infectivity and disease-associated protease-resistant prion protein (PrPres) were both generated under cell-free conditions, which supported a nonviral hypothesis for the agent. However, these studies lacked comparative quantitation of both infectivity titers and PrPres, which is important both for biological comparison with in vivo-derived infectivity and for excluding contamination to explain the results. Here during four to eight rounds of PMCA, end-point dilution titrations detected a >320-fold increase in infectivity versus that in controls. These results provide strong support for the hypothesis that the agent of prion infectivity is not a virus. PMCA-generated samples caused the same clinical disease and neuropathology with the same rapid incubation period as the input brain-derived scrapie samples, providing no evidence for generation of a new strain in PMCA. However, the ratio of the infectivity titer to the amount of PrPres (specific infectivity) was much lower in PMCA versus brain-derived samples, suggesting the possibility that a substantial portion of PrPres generated in PMCA might be noninfectious.
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