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    Prion strain-specific structure and pathology: A view from the perspective of glycobiology

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    Author
    Baskakov, I.V.
    Katorcha, E.
    Makarava, N.
    Date
    2018
    Journal
    Viruses
    Publisher
    MDPI AG
    Type
    Review
    
    Metadata
    Show full item record
    See at
    https://dx.doi.org/10.3390/v10120723
    Abstract
    Prion diseases display multiple disease phenotypes characterized by diverse clinical symptoms, different brain regions affected by the disease, distinct cell tropism and diverse PrP Sc deposition patterns. The diversity of disease phenotypes within the same host is attributed to the ability of PrP C to acquire multiple, alternative, conformationally distinct, self-replicating PrP Sc states referred to as prion strains or subtypes. Structural diversity of PrP Sc strains has been well documented, yet the question of how different PrP Sc structures elicit multiple disease phenotypes remains poorly understood. The current article reviews emerging evidence suggesting that carbohydrates in the form of sialylated N-linked glycans, which are a constitutive part of PrP Sc , are important players in defining strain-specific structures and disease phenotypes. This article introduces a new hypothesis, according to which individual strain-specific PrP Sc structures govern selection of PrP C sialoglycoforms that form strain-specific patterns of carbohydrate epitopes on PrP Sc surface and contribute to defining the disease phenotype and outcomes. � 2018 by the authors. Licensee MDPI, Basel, Switzerland.
    Sponsors
    Funding: Financial support for this study was provided by National Institute of Health Grants R01 NS045585 and R01 AI128925.
    Keyword
    Glycosylation
    N-linked glycans
    Prion disease
    Prion strains
    Prions
    Sialic acid
    Sialylation
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85058883953&doi=10.3390%2fv10120723&partnerID=40&md5=161880db61ae9d444276a57b78289e84; http://hdl.handle.net/10713/8832
    ae974a485f413a2113503eed53cd6c53
    10.3390/v10120723
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    UMB Open Access Articles 2018

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