• Login
    View Item 
    •   Home
    • Articles and other publications by RIVM employees
    • Miscellaneous
    • View Item
    •   Home
    • Articles and other publications by RIVM employees
    • Miscellaneous
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    RIVM Publications RepositoryCommunitiesTitleAuthorsIssue DateSubmit Date

    My Account

    LoginRegister

    Statistics

    Display statistics

    Stable isotope tagging of epitopes: a highly selective strategy for the identification of major histocompatibility complex class I-associated peptides induced upon viral infection.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    meiring.pdf
    Size:
    1.051Mb
    Format:
    PDF
    Download
    Average rating
     
       votes
    Cast your vote
    You can rate an item by clicking the amount of stars they wish to award to this item. When enough users have cast their vote on this item, the average rating will also be shown.
    Star rating
     
    Your vote was cast
    Thank you for your feedback
    Authors
    Meiring, Hugo D
    Soethout, Ernst C
    Poelen, Martien C M
    Mooibroek, Dennis
    Hoogerbrugge, Ronald
    Timmermans, Hans
    Boog, Claire J
    Heck, Albert J R
    Jong, Ad P J M de
    Els, Cécile A C M van
    Type
    Article
    Language
    en
    
    Metadata
    Show full item record
    Title
    Stable isotope tagging of epitopes: a highly selective strategy for the identification of major histocompatibility complex class I-associated peptides induced upon viral infection.
    Publiekssamenvatting
    Identification of peptides presented in major histocompatibility complex (MHC) class I molecules after viral infection is of strategic importance for vaccine development. Until recently, mass spectrometric identification of virus-induced peptides was based on comparative analysis of peptide pools isolated from uninfected and virus-infected cells. Here we report on a powerful strategy aiming at the rapid, unambiguous identification of naturally processed MHC class I-associated peptides, which are induced by viral infection. The methodology, stable isotope tagging of epitopes (SITE), is based on metabolic labeling of endogenously synthesized proteins during infection. This is accomplished by culturing virus-infected cells with stable isotope-labeled amino acids that are expected to be anchor residues (i.e. residues of the peptide that have amino acid side chains that bind into pockets lining the peptide-binding groove of the MHC class I molecule) for the human leukocyte antigen allele of interest. Subsequently these cells are mixed with an equal number of non-infected cells, which are cultured in normal medium. Finally peptides are acid-eluted from immunoprecipitated MHC molecules and subjected to two-dimensional nanoscale LC-MS analysis. Virus-induced peptides are identified through computer-assisted detection of characteristic, binomially distributed ratios of labeled and unlabeled molecules. Using this approach we identified novel measles virus and respiratory syncytial virus epitopes as well as infection-induced self-peptides in several cell types, showing that SITE is a unique and versatile method for unequivocal identification of disease-related MHC class I epitopes.
    DOI
    10.1074/mcp.T500014-MCP200
    PMID
    16432254
    URI
    http://hdl.handle.net/10029/8396
    ae974a485f413a2113503eed53cd6c53
    10.1074/mcp.T500014-MCP200
    Scopus Count
    Collections
    Miscellaneous

    entitlement

    Related articles

    • Targeted identification of infection-related HLA class I-presented epitopes by stable isotope tagging of epitopes (SITE).
    • Authors: Meiring HD, Soethout EC, de Jong APJM, van Els CACM
    • Issue date: 2007 May
    • A microcapillary column switching HPLC-electrospray ionization MS system for the direct identification of peptides presented by major histocompatibility complex class I molecules.
    • Authors: van der Heeft E, ten Hove GJ, Herberts CA, Meiring HD, van Els CA, de Jong AP
    • Issue date: 1998 Sep 15
    • Rapid and sensitive identification of major histocompatibility complex class I-associated tumor peptides by Nano-LC MALDI MS/MS.
    • Authors: Hofmann S, Glückmann M, Kausche S, Schmidt A, Corvey C, Lichtenfels R, Huber C, Albrecht C, Karas M, Herr W
    • Issue date: 2005 Dec
    • The canine MHC class Ia allele DLA-88*508:01 presents diverse self- and canine distemper virus-origin peptides of varying length that have a conserved binding motif.
    • Authors: Ross P, Nemec PS, Kapatos A, Miller KR, Holmes JC, Suter SE, Buntzman AS, Soderblom EJ, Collins EJ, Hess PR
    • Issue date: 2018 Mar
    • Endogenous presentation of a nascent antigenic epitope to CD8+ CTL is more efficient than exogenous presentation.
    • Authors: Hahn YS, Hahn CS, Braciale TJ
    • Issue date: 1996 Oct

    DSpace software (copyright © 2002 - 2023)  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.