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    Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2

    Access Status
    Fulltext not available
    Authors
    Katsara, M.
    Yuriev, E.
    Ramsland, Paul
    Deraos, G.
    Tselios, T.
    Matsoukas, J.
    Apostolopoulos, V.
    Date
    2008
    Type
    Journal Article
    
    Metadata
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    Citation
    Katsara, M. and Yuriev, E. and Ramsland, P. and Deraos, G. and Tselios, T. and Matsoukas, J. and Apostolopoulos, V. 2008. Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2. Molecular Immunology. 45 (13): pp. 3661-3670.
    Source Title
    Molecular Immunology
    DOI
    10.1016/j.molimm.2008.04.024
    ISSN
    0161-5890
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/47052
    Collection
    • Curtin Research Publications
    Abstract

    Multiple sclerosis (MS) is an autoimmune demyelinating disease mediated primarily by CD4+ T cells. The design of peptide mutants of disease-associated myelin epitopes to alter immune responses offers a promising avenue for the treatment of MS. We designed and synthesized a number of peptide analogs by mutating the principal TCR contact residue based on MBP83-99 epitope and these peptides were conjugated to reduced mannan. Immune responses were diverted from Th1 to Th2 in SJL/J mice and generated antibodies which did not cross-react with native MBP protein. Peptide [Y91]MBP83-99 gave the best cytokine and antibody profile and constitutes a promising candidate peptide for immunotherapy of MS. Structural alignment of existing crystal structures revealed the peptide binding motif of I-As. Molecular modeling was used to identify H-bonding and van der Waals interactions between peptides and MHC (I-As). © 2008 Elsevier Ltd. All rights reserved.

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