ArticleJournal of cellular biochemistry2011
High CJD infectivity remains after prion protein is destroyed.
Article in Journal of cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C).PLoS pathogens · 2012Trial
- "Prion-like" seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders.Frontiers in neuroscience · 2024Review
- Prion disease modelled in Drosophila.Cell and tissue research · 2023Review
- Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein.Veterinary research · 2021Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Viral Infections and Obesity.Current obesity reports · 2017Review
- Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.PloS one · 2017Article
- Proteomic analysis of host brain components that bind to infectious particles in Creutzfeldt-Jakob disease.Proteomics · 2015Article
- Synthetic scrapie infectivity: interaction between recombinant PrP and scrapie brain-derived RNA.Virulence · 2015Article
- Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions.Prion · 2015Article
- Rapid chemical decontamination of infectious CJD and scrapie particles parallels treatments known to disrupt microbes and biofilms.Virulence · 2015Article
- Highly infectious CJD particles lack prion protein but contain many viral-linked peptides by LC-MS/MS.Journal of cellular biochemistry · 2014Article
- Dissociation of prion protein amyloid seeding from transmission of a spongiform encephalopathy.Journal of virology · 2013Article
- Evaluation of a combinatorial approach to prion inactivation using an oxidizing agent, SDS, and proteinase K.BMC veterinary research · 2013Article
- Review
- Cellular aspects of prion replication in vitro.Viruses · 2013Review
- Exposure of RML scrapie agent to a sodium percarbonate-based product and sodium dodecyl sulfate renders PrPSc protease sensitive but does not eliminate infectivity.BMC veterinary research · 2013Article
- Article
- Viruses do replicate in cell-free systems.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Continuous production of prions after infectious particles are eliminated: implications for Alzheimer's disease.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The hypothesis that host prion protein (PrP) converts into an infectious prion form rests on the observation that infectivity progressively decreases in direct proportion to the decrease of PrP with proteinase K (PK) treatment. PrP that resists limited PK digestion (PrP-res, PrP(sc)) has been assumed to be the infectious form, with speculative types of misfolding encoding the many unique transmissible spongiform encephalopathy (TSE) agent strains. Recently, a PK sensitive form of PrP has been proposed as the prion. Thus we re-evaluated total PrP (sensitive and resistant) and used a cell-based assay for titration of infectious particles. A keratinase (NAP) known to effectively digest PrP was compared to PK. Total PrP in FU-CJD infected brain was reduced to ≤0.3% in a 2 h PK digest, yet there was no reduction in titer. Remaining non-PrP proteins were easily visualized with colloidal gold in this highly infectious homogenate. In contrast to PK, NAP digestion left 0.8% residual PrP after 2 h, yet decreased titer by >2.5 log; few residual protein bands remained. FU-CJD infected cells with 10× the infectivity of brain by both animal and cell culture assays were also evaluated. NAP again significantly reduced cell infectivity (>3.5 log). Extreme PK digestions were needed to reduce cell PrP to <0.2%, yet a very high titer of 8 logs survived. Our FU-CJD brain results are in good accord with the only other report on maximal PrP destruction and titer. It is likely that one or more residual non-PrP proteins may protect agent nucleic acids in infectious particles.
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What OpenQuestion holds
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.