• 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

    Arginine (Di)methylated Human Leukocyte Antigen Class I Peptides Are Favorably Presented by HLA-B*07.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    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
    Marino, Fabio
    Mommen, Geert P M
    Jeko, Anita
    Meiring, Hugo D
    van Gaans-van den Brink, Jacqueline A M
    Scheltema, Richard A
    van Els, Cécile A C M
    Heck, Albert J R
    Type
    Article
    Language
    en
    
    Metadata
    Show full item record
    Title
    Arginine (Di)methylated Human Leukocyte Antigen Class I Peptides Are Favorably Presented by HLA-B*07.
    Published in
    J Proteome Res 2017; 16(1):34-44
    Publiekssamenvatting
    Alterations in protein post-translational modification (PTM) are recognized hallmarks of diseases. These modifications potentially provide a unique source of disease-related human leukocyte antigen (HLA) class I-presented peptides that can elicit specific immune responses. While phosphorylated HLA peptides have already received attention, arginine methylated HLA class I peptide presentation has not been characterized in detail. In a human B-cell line we detected 149 HLA class I peptides harboring mono- and/or dimethylated arginine residues by mass spectrometry. A striking preference was observed in the presentation of arginine (di)methylated peptides for HLA-B*07 molecules, likely because the binding motifs of this allele resemble consensus sequences recognized by arginine methyl-transferases. Moreover, HLA-B*07-bound peptides preferentially harbored dimethylated groups at the P3 position, thus consecutively to the proline anchor residue. Such a proline-arginine sequence has been associated with the arginine methyl-transferases CARM1 and PRMT5. Making use of the specific neutral losses in fragmentation spectra, we found most of the peptides to be asymmetrically dimethylated, most likely by CARM1. These data expand our knowledge of the processing and presentation of arginine (di)methylated HLA class I peptides and demonstrate that these types of modified peptides can be presented for recognition by T-cells. HLA class I peptides with mono- and dimethylated arginine residues may therefore offer a novel target for immunotherapy.
    DOI
    10.1021/acs.jproteome.6b00528
    PMID
    27503676
    URI
    http://hdl.handle.net/10029/621697
    ae974a485f413a2113503eed53cd6c53
    10.1021/acs.jproteome.6b00528
    Scopus Count
    Collections
    Miscellaneous

    entitlement

    Related articles

    • Synthesis and biological evaluation of two chemically modified peptide epitopes for the class I MHC protein HLA-B*2705.
    • Authors: Jones MA, Hislop AD, Snaith JS
    • Issue date: 2006 Oct 21
    • The HLA Ligandome Comprises a Limited Repertoire of O-GlcNAcylated Antigens Preferentially Associated With HLA-B*07:02.
    • Authors: Mukherjee S, Sanchez-Bernabeu A, Demmers LC, Wu W, Heck AJR
    • Issue date: 2021
    • A proteomic analysis of arginine-methylated protein complexes.
    • Authors: Boisvert FM, Côté J, Boulanger MC, Richard S
    • Issue date: 2003 Dec
    • TDRD3 is an effector molecule for arginine-methylated histone marks.
    • Authors: Yang Y, Lu Y, Espejo A, Wu J, Xu W, Liang S, Bedford MT
    • Issue date: 2010 Dec 22
    • Nη-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases.
    • Authors: Lakowski TM, 't Hart P, Ahern CA, Martin NI, Frankel A
    • Issue date: 2010 Nov 19

    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.