ArticleBiochemistry2014
Prion nucleation site unmasked by transient interaction with phospholipid cofactor.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins.PloS one · 2021Article
- Liquid and Hydrogel Phases of PrPMolecular cell · 2018Article
- Prion replication environment defines the fate of prion strain adaptation.PLoS pathogens · 2018Article
- Mutations Alter RNA-Mediated Conversion of Human Prions.ACS omega · 2018Article
- Molecular dynamics simulations of early steps in RNA-mediated conversion of prions.Protein science : a publication of the Protein Society · 2017Article
- Selective propagation of mouse-passaged scrapie prions with long incubation period from a mixed prion population using GT1-7 cells.PloS one · 2017Article
- Role of polysaccharide and lipid in lipopolysaccharide induced prion protein conversion.Prion · 2016Article
- PrP charge structure encodes interdomain interactions.Scientific reports · 2015Article
- Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein.PloS one · 2015Article
- Neutron reflectometry studies define prion protein N-terminal peptide membrane binding.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Infectious mammalian prions can be formed de novo from purified recombinant prion protein (PrP) substrate through a pathway that requires the sequential addition of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG) and RNA cofactor molecules. Recent studies show that the initial interaction between PrP and POPG causes widespread and persistent conformational changes to form an insoluble intermediate species, termed PrP(Int1). Here, we characterize the mechanism and functional consequences of the interaction between POPG and PrP. Negative-stain electron microscopy of PrP(Int1) revealed the presence of amorphous aggregates. Pull-down and photoaffinity label experiments indicate that POPG induces the formation of a PrP(C) polybasic-domain-binding neoepitope within PrP(Int1). The ongoing presence of POPG is not required to maintain PrP(Int1) structure, as indicated by the absence of stoichiometric levels of POPG in solid-state NMR measurements of PrP(Int1). Together, these results show that a transient interaction with POPG cofactor unmasks a PrP(C) binding site, leading to PrP(Int1) aggregation.
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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.