ArticlePLoS pathogens2011
Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 48 citations in OpenAlex.
- A scalable, dividing cell model for the robust propagation and quantification of human sporadic Creutzfeldt-Jakob disease prions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Neuropathologically directed profiling of PRNP somatic and germline variants in sporadic human prion disease.Acta neuropathologica · 2024Article
- Neuropathologically-directed profiling ofbioRxiv : the preprint server for biology · 2024Article
- The manifold role of octapeptide repeats in prion protein assembly.Peptide science (Hoboken, N.J.) · 2023Article
- Early Stages of RNA-Mediated Conversion of Human Prions.The journal of physical chemistry. B · 2022Article
- A single amino acid residue in bank vole prion protein drives permissiveness to Nor98/atypical scrapie and the emergence of multiple strain variants.PLoS pathogens · 2022Article
- Brain Somatic Mutation in Aging and Alzheimer's Disease.Annual review of genomics and human genetics · 2021Review
- Isolation of infectious, non-fibrillar and oligomeric prions from a genetic prion disease.Brain : a journal of neurology · 2020Article
- Cellulose ether treatment in vivo generates chronic wasting disease prions with reduced protease resistance and delayed disease progression.Journal of neurochemistry · 2020Article
- Article
- Alteration of Prion Strain Emergence by Nonhost Factors.mSphere · 2019Article
- Altered Domain Structure of the Prion Protein Caused by CuStructure (London, England : 1993) · 2019Article
- Prion neurotoxicity.Brain pathology (Zurich, Switzerland) · 2019Review
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.Scientific reports · 2018Article
- Mutations Alter RNA-Mediated Conversion of Human Prions.ACS omega · 2018Article
- Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.PLoS pathogens · 2017Article
- Molecular dynamics simulations of early steps in RNA-mediated conversion of prions.Protein science : a publication of the Protein Society · 2017Article
- Identification of Anti-prion Compounds using a Novel Cellular Assay.The Journal of biological chemistry · 2016Article
- Isolation of a Defective Prion Mutant from Natural Scrapie.PLoS pathogens · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies identified two mammalian prion protein (PrP) polybasic domains that bind the disease-associated conformer PrP(Sc), suggesting that these domains of cellular prion protein (PrP(C)) serve as docking sites for PrP(Sc) during prion propagation. To examine the role of polybasic domains in the context of full-length PrP(C), we used prion proteins lacking one or both polybasic domains expressed from Chinese hamster ovary (CHO) cells as substrates in serial protein misfolding cyclic amplification (sPMCA) reactions. After ∼5 rounds of sPMCA, PrP(Sc) molecules lacking the central polybasic domain (ΔC) were formed. Surprisingly, in contrast to wild-type prions, ΔC-PrP(Sc) prions could bind to and induce quantitative conversion of all the polybasic domain mutant substrates into PrP(Sc) molecules. Remarkably, ΔC-PrP(Sc) and other polybasic domain PrP(Sc) molecules displayed diminished or absent biological infectivity relative to wild-type PrP(Sc), despite their ability to seed sPMCA reactions of normal mouse brain homogenate. Thus, ΔC-PrP(Sc) prions interact with PrP(C) molecules through a novel interaction mechanism, yielding an expanded substrate range and highly efficient PrP(Sc) propagation. Furthermore, polybasic domain deficient PrP(Sc) molecules provide the first example of dissociation between normal brain homogenate sPMCA seeding ability from biological prion infectivity. These results suggest that the propagation of PrP(Sc) molecules may not depend on a single stereotypic mechanism, but that normal PrP(C)/PrP(Sc) interaction through polybasic domains may be required to generate prion infectivity.
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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.