ArticleScientific reports2015
Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- BoDV-1 Infection Is Associated with Altered Prion Protein Glycoform Maturation and Reduced ETS1-MGAT5/GnTV Pathway Activity in Rat C6 Astroglial Cells.Microorganisms · 2026Article
- Genome-wide screens identify core regulators of cell surface prion protein expression.Scientific reports · 2026Article
- Oligosaccharyltransferase (OST) complex inhibition effectively treats rodent and human prions.PLoS pathogens · 2026Article
- Reactive Microglia and Astrocytes as Therapeutic Targets in Prion Diseases.Sub-cellular biochemistry · 2025Review
- Biological function of sialic acid and sialylation in human health and disease.Cell death discovery · 2024Review
- Multiple steps of prion strain adaptation to a new host.Frontiers in neuroscience · 2024Article
- Post-translational modifications in prion diseases.Frontiers in molecular neuroscience · 2024Review
- Reactive astrocytes associated with prion disease impair the blood brain barrier.Neurobiology of disease · 2023Article
- Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake.Journal of biochemistry · 2023Article
- A point mutation in GPI-attachment signal peptide accelerates the development of prion disease.Acta neuropathologica · 2023Article
- Role of sialylation of N-linked glycans in prion pathogenesis.Cell and tissue research · 2023Review
- Cell biology of prion strains in vivo and in vitro.Cell and tissue research · 2023Review
- Reactive astrocytes associated with prion disease impair the blood brain barrier.bioRxiv : the preprint server for biology · 2023Article
- Review
- Deficiency in ST6GAL1, one of the two α2,6-sialyltransferases, has only a minor effect on the pathogenesis of prion disease.Frontiers in molecular biosciences · 2022Article
- Review
- Potential for transmission of sporadic Creutzfeldt-Jakob disease through peripheral routes.Laboratory investigation; a journal of technical methods and pathology · 2021Article
- Article
- Efficient interspecies transmission of synthetic prions.PLoS pathogens · 2021Article
- Asymmetric-flow field-flow fractionation of prions reveals a strain-specific continuum of quaternary structures with protease resistance developing at a hydrodynamic radius of 15 nm.PLoS pathogens · 2021Article
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4 authors.
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Abstract
Prion or PrP(Sc) is a proteinaceous infectious agent that consists of a misfolded and aggregated form of a sialoglycoprotein called prion protein or PrP(C). PrP(C) has two sialylated N-linked carbohydrates. In PrP(Sc), the glycans are directed outward, with the terminal sialic acid residues creating a negative charge on the surface of prion particles. The current study proposes a new hypothesis that electrostatic repulsion between sialic residues creates structural constraints that control prion replication and PrP(Sc) glycoform ratio. In support of this hypothesis, here we show that diglycosylated PrP(C) molecules that have more sialic groups per molecule than monoglycosylated PrP(C) were preferentially excluded from conversion. However, when partially desialylated PrP(C) was used as a substrate, recruitment of three glycoforms into PrP(Sc) was found to be proportional to their respective populations in the substrate. In addition, hypersialylated molecules were also excluded from conversion in the strains with the strongest structural constraints, a strategy that helped reduce electrostatic repulsion. Moreover, as predicted by the hypothesis, partial desialylation of PrP(C) significantly increased the replication rate. This study illustrates that sialylation of N-linked glycans creates a prion replication barrier that controls replication rate and glycoform ratios and has broad implications.
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