• Login
    View Item 
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of ChristieCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsProfilesView

    My Account

    LoginRegister

    Local Links

    The Christie WebsiteChristie Library and Knowledge Service

    Statistics

    Display statistics

    The processing, transport and heterologous expression of Epstein-Barr virus gp110.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Papworth, Monika A
    Van Dijk, Albie A
    Benyon, Gordon R
    Allen, Terence D
    Arrand, John R
    Mackett, Mike
    Affiliation
    CRC Department of Molecular Biology, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Withington, Manchester, UK.
    Issue Date
    1997-09
    
    Metadata
    Show full item record
    Abstract
    Epstein-Barr virus (EBV) glycoprotein gp110 has substantial structural and sequence homology with herpes simplex virus (HSV) gB and gBs of other alpha- and betaherpesviruses but unlike HSV gB localizes differently in infected cells and is absent from virions. To facilitate the analysis of EBV gp110, antisera were raised to fragments of gp110 expressed in a bacterial system. They recognized a protein of the predicted size in recombinant bacterial lysates, in lymphoblastoid cells and in recombinant vaccinia virus-gp110 infected cells. gp110 from all sources possessed a high-mannose type of N-glycosylation implying that gp110 has not passed through the Golgi. Immunofluorescence and immuno-electron microscopy confirmed this conclusion and demonstrated that, in contrast to HSV gB, the majority of immunoreactive gp110 was present at the nuclear membrane or endoplasmic reticulum (ER) but not at the cell membrane. Unexpectedly, a truncated version of gp110 lacking the hydrophobic C-terminal region, despite forming dimers analogous to HSV dimers, was transported in a similar manner to full-length gp110. Two chimeric proteins constructed by replacing the N- and C-terminal domains of gp110 with corresponding regions of gp340/220 were also transported to the nuclear membrane/ER. These data suggest that unlike HSV gB both the N- and C-terminal portions of EBV gp110 contain independent signals sufficient to direct the molecule to the ER/nuclear membrane. Specific transport of gammaherpesvirus gB homologues to the nuclear membrane, from where herpesviruses bud, suggests that they may be involved in the egress of virus from the nucleus.
    Citation
    The processing, transport and heterologous expression of Epstein-Barr virus gp110. 1997, 78 ( Pt 9):2179-89 J. Gen. Virol.
    Journal
    The Journal of General Virology
    URI
    http://hdl.handle.net/10541/95237
    PubMed ID
    9292005
    Type
    Article
    Language
    en
    ISSN
    0022-1317
    Collections
    All Paterson Institute for Cancer Research

    entitlement

    Related articles

    • Four consecutive arginine residues at positions 836-839 of EBV gp110 determine intracellular localization of gp110.
    • Authors: Lee SK
    • Issue date: 1999 Nov 25
    • Membrane binding properties of EBV gp110 C-terminal domain; evidences for structural transition in the membrane environment.
    • Authors: Park SJ, Seo MD, Lee SK, Lee BJ
    • Issue date: 2008 Sep 30
    • Failure to complement infectivity of EBV and HSV-1 glycoprotein B (gB) deletion mutants with gBs from different human herpesvirus subfamilies.
    • Authors: Lee SK, Compton T, Longnecker R
    • Issue date: 1997 Oct 13
    • Human herpesvirus-8 glycoprotein B interacts with Epstein-Barr virus (EBV) glycoprotein 110 but fails to complement the infectivity of EBV mutants.
    • Authors: Pertel PE, Spear PG, Longnecker R
    • Issue date: 1998 Nov 25
    • Characterization of murine gammaherpesvirus 68 glycoprotein B (gB) homolog: similarity to Epstein-Barr virus gB (gp110).
    • Authors: Stewart JP, Janjua NJ, Sunil-Chandra NP, Nash AA, Arrand JR
    • Issue date: 1994 Oct
    DSpace software (copyright © 2002 - 2025)  DuraSpace
    Quick Guide | Contact Us
    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.