ArticleProceedings of the National Academy of Sciences of the United States of America2015
Post-conversion sialylation of prions in lymphoid tissues.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 46 citations in OpenAlex.
- Distinct prion conformers from brain and peripheral tissues of gene-targeted mice produce convergent CWD strain properties.PLoS pathogens · 2026Article
- Bovine Spongiform Encephalopathy: An Integrated Review of Prion Mechanisms, Neuroanatomy, and Control.Veterinary sciences · 2026Review
- Cases of Creutzfeldt-Jakob disease in young individuals: open questions regarding aetiology.Frontiers in cellular neuroscience · 2025Article
- Post-translational modifications in prion diseases.Frontiers in molecular neuroscience · 2024Review
- Multiple steps of prion strain adaptation to a new host.Frontiers in neuroscience · 2024Article
- Reactive astrocytes associated with prion disease impair the blood brain barrier.Neurobiology of disease · 2023Article
- 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
- Does SIGLEC8 localize to the subcellular compartment like the Alzheimer's disease protective CD33 splice variant?Frontiers in cellular neuroscience · 2023Article
- 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
- The degree of astrocyte activation is predictive of the incubation time to prion disease.Acta neuropathologica communications · 2021Article
- Involvement of Cellular Prion Protein in Invasion and Metastasis of Lung Cancer by Inducing Treg Cell Development.Biomolecules · 2021Article
- From Posttranslational Modifications to Disease Phenotype: A Substrate Selection Hypothesis in Neurodegenerative Diseases.International journal of molecular sciences · 2021Review
- Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different cell tropism.Neurobiology of disease · 2020Article
- Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism.International journal of molecular sciences · 2020Article
- Unaltered intravenous prion disease pathogenesis in the temporary absence of marginal zone B cells.Scientific reports · 2019Article
- Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Sialylated glycans on the surface of mammalian cells act as part of a "self-associated molecular pattern," helping the immune system to recognize "self" from "altered self" or "nonself." To escape the host immune system, some bacterial pathogens have evolved biosynthetic pathways for host-like sialic acids, whereas others recruited host sialic acids for decorating their surfaces. Prions lack nucleic acids and are not conventional pathogens. Nevertheless, prions might use a similar strategy for invading and colonizing the lymphoreticular system. Here we show that the sialylation status of the infectious, disease-associated state of the prion protein (PrP(Sc)) changes with colonization of secondary lymphoid organs (SLOs). As a result, spleen-derived PrP(Sc) is more sialylated than brain-derived PrP(Sc). Enhanced sialylation of PrP(Sc) is recapitulated in vitro by incubating brain-derived PrP(Sc) with primary splenocytes or cultured macrophage RAW 264.7 cells. General inhibitors of sialyltranserases (STs), the enzymes that transfer sialic acid residues onto terminal positions of glycans, suppressed extrasialylation of PrP(Sc). A fluorescently labeled precursor of sialic acid revealed ST activity associated with RAW macrophages. This study illustrates that, upon colonization of SLOs, the sialylation status of prions changes by host STs. We propose that this mechanism is responsible for camouflaging prions in SLOs and has broad implications.
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