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  1. Article: Maturation of Borna disease virus glycoprotein

    Eickmann, Markus / Kiermayer, Simone / Kraus, Ina / Gossl, Melanie / Richt, Jurgen A / Garten, Wolfgang

    FEBS letters. 2005 Aug. 29, v. 579, no. 21

    2005  

    Abstract: The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) ... ...

    Abstract The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) predominantly located in the endoplasmic reticulum (ER), (ii) partially exists in the ER already as cleaved subunits GP-N and GP-C, (iii) is directed to the ER/cis-Golgi region by its transmembrane and/or cytoplasmic domains in CD8-BDV-GP hybrid constructs and (iv) is incorporated in the virus particles as authentic BDV glycoprotein exclusively in the cleaved form decorated with N-glycans of the complex type. Downregulation of BDV-glycoproteins on the cell surface, their limited proteolytic processing, and protection of antigenic epitopes on the viral glycoproteins by host-identical N-glycans are different strategies for persistent virus infections.
    Keywords Borna disease virus ; viral proteins ; glycoproteins ; virus replication ; endoplasmic reticulum ; cytochemistry ; protein transport ; polysaccharides ; epitopes ; host-pathogen relationships
    Language English
    Dates of publication 2005-0829
    Size p. 4751-4756.
    Document type Article
    DOI 10.1016/j.febslet.2005.07.052
    Database NAL-Catalogue (AGRICOLA)

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  2. Article: Maturation of Borna disease virus glycoprotein.

    Eickmann, Markus / Kiermayer, Simone / Kraus, Ina / Gössl, Melanie / Richt, Jürgen A / Garten, Wolfgang

    FEBS letters

    2005  Volume 579, Issue 21, Page(s) 4751–4756

    Abstract: The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) ... ...

    Abstract The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) predominantly located in the endoplasmic reticulum (ER), (ii) partially exists in the ER already as cleaved subunits GP-N and GP-C, (iii) is directed to the ER/cis-Golgi region by its transmembrane and/or cytoplasmic domains in CD8-BDV-GP hybrid constructs and (iv) is incorporated in the virus particles as authentic BDV glycoprotein exclusively in the cleaved form decorated with N-glycans of the complex type. Downregulation of BDV-glycoproteins on the cell surface, their limited proteolytic processing, and protection of antigenic epitopes on the viral glycoproteins by host-identical N-glycans are different strategies for persistent virus infections.
    MeSH term(s) Animals ; Borna disease virus/metabolism ; COS Cells ; Cercopithecus aethiops ; Endoplasmic Reticulum/metabolism ; Epitopes ; Protein Structure, Tertiary ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Viral Fusion Proteins/genetics ; Viral Fusion Proteins/metabolism
    Chemical Substances Epitopes ; Protein Subunits ; Recombinant Fusion Proteins ; Viral Fusion Proteins
    Language English
    Publishing date 2005-08-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2005.07.052
    Database MEDical Literature Analysis and Retrieval System OnLINE

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