ArticleMolecular neurodegeneration2012
Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPres level disparity.
Article in Molecular neurodegeneration, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- PrPSc Oligomerization Appears Dynamic, Quickly Engendering Inherent M1000 Acute Synaptotoxicity.Biophysical journal · 2020Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Thermostability as a highly dependent prion strain feature.Scientific reports · 2019Article
- Early existence and biochemical evolution characterise acutely synaptotoxic PrPSc.PLoS pathogens · 2019Article
- Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species.PLoS pathogens · 2018Article
- Prion protein "gamma-cleavage": characterizing a novel endoproteolytic processing event.Cellular and molecular life sciences : CMLS · 2016Article
- MEK1 transduces the prion protein N2 fragment antioxidant effects.Cellular and molecular life sciences : CMLS · 2015Article
- Shedding light on prion disease.Prion · 2015Article
- Synthetic scrapie infectivity: interaction between recombinant PrP and scrapie brain-derived RNA.Virulence · 2015Article
- Prion infection impairs cholesterol metabolism in neuronal cells.The Journal of biological chemistry · 2014Article
- Myositis facilitates preclinical accumulation of pathological prion protein in muscle.Acta neuropathologica communications · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPrion disease transmission and pathogenesis are linked to misfolded, typically protease resistant (PrPres) conformers of the normal cellular prion protein (PrPC), with the former posited to be the principal constituent of the infectious 'prion'. Unexplained discrepancies observed between detectable PrPres and infectivity levels exemplify the complexity in deciphering the exact biophysical nature of prions and those host cell factors, if any, which contribute to transmission efficiency. In order to improve our understanding of these important issues, this study utilized a bioassay validated cell culture model of prion infection to investigate discordance between PrPres levels and infectivity titres at a subcellular resolution.
findingsSubcellular fractions enriched in lipid rafts or endoplasmic reticulum/mitochondrial marker proteins were equally highly efficient at prion transmission, despite lipid raft fractions containing up to eight times the levels of detectable PrPres. Brain homogenate infectivity was not differentially enhanced by subcellular fraction-specific co-factors, and proteinase K pre-treatment of selected fractions modestly, but equally reduced infectivity. Only lipid raft associated infectivity was enhanced by sonication.
conclusionsThis study authenticates a subcellular disparity in PrPres and infectivity levels, and eliminates simultaneous divergence of prion strains as the explanation for this phenomenon. On balance, the results align best with the concept that transmission efficiency is influenced more by intrinsic characteristics of the infectious prion, rather than cellular microenvironment conditions or absolute PrPres levels.
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