• Login
    View Item 
    •   UMB Digital Archive
    • UMB Open Access Articles
    • UMB Open Access Articles 2017
    • View Item
    •   UMB Digital Archive
    • UMB Open Access Articles
    • UMB Open Access Articles 2017
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UMB Digital ArchiveCommunitiesPublication DateAuthorsTitlesSubjectsThis CollectionPublication DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    Statistics

    Display statistics

    Analyses of N-linked glycans of PrPSc revealed predominantly 2,6-linked sialic acid residues

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Author
    Katorcha, E.
    Baskakov, I.V.
    Date
    2017
    Journal
    FEBS Journal
    Publisher
    Blackwell Publishing Ltd
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://doi.org/10.1111/febs.14268
    Abstract
    Mammalian prions (PrPSc) consist of misfolded, conformationally altered, self-replicating states of the sialoglycoprotein called prion protein or PrPC. Recent studies revealed that the sialylation status of PrPSc plays a major role in evading innate immunity and infecting a host. Establishing the type of linkage by which sialic acid residues are attached to galactose is important, as it helps to identify the sialyltransferases responsible for sialylating PrPC and outline strategies for manipulating the sialyation status of PrPSc. Using enzymatic treatment with sialidases and lectin blots, this study demonstrated that in N-linked glycans of PrPSc, the sialic acid residues are predominantly alpha 2,6-linked. High percentages of alpha 2,6-linked sialic acids were observed in PrPSc of three prion strains 22L, RML, and ME7, as well as PrPSc from brain, spleen, or N2a cells cultured in vitro. Moreover, the variation in the percentage of alpha 2,3- versus 2,6-linked sialic acid was found to be relatively minor between brain-, spleen-, or cell-derived PrPSc, suggesting that the type of linkage is independent of tissue type. Based on the current results, we propose that sialyltransferases of St6Gal family, which is responsible for attaching sialic acids via alpha 2,6-linkages to N-linked glycans, controls sialylation of PrPC and PrPSc.
    Sponsors
    This study was carried out in strict accordance with the recommendations in the Guide for the Care and Use of Laboratory Animals of the National Institutes of Health. The animal protocol was approved by the Institutional Animal Care and Use Committee of the University of Maryland, Baltimore (assurance no. A32000-01, permit no. 0215002).
    Keyword
    lectin
    N-linked glycans
    prion protein
    sialidase
    sialylation
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85033385873&doi=10.1111%2ffebs.14268&partnerID=40&md5=f7c3512830e3dd8859253984cb00bf36; http://hdl.handle.net/10713/10963
    ae974a485f413a2113503eed53cd6c53
    10.1111/febs.14268
    Scopus Count
    Collections
    UMB Open Access Articles 2017

    entitlement

    Related articles

    • Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology.
    • Authors: Baskakov IV
    • Issue date: 2017 Mar 4
    • Sialylation Controls Prion Fate <i>in Vivo</i>.
    • Authors: Srivastava S, Katorcha E, Daus ML, Lasch P, Beekes M, Baskakov IV
    • Issue date: 2017 Feb 10
    • Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity.
    • Authors: Katorcha E, Makarava N, Savtchenko R, D'Azzo A, Baskakov IV
    • Issue date: 2014 Sep
    • Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio.
    • Authors: Katorcha E, Makarava N, Savtchenko R, Baskakov IV
    • Issue date: 2015 Nov 18
    • Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism.
    • Authors: Makarava N, Chang JC, Baskakov IV
    • Issue date: 2020 Jan 28
    DSpace software (copyright © 2002 - 2021)  DuraSpace
    Quick Guide | Policies | Contact Us | UMB Health Sciences & Human Services Library
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.