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    A double mutation of MBP83-99 peptide induces IL-4 responses and antagonizes IFN-? responses

    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. A double mutation of MBP83-99 peptide induces IL-4 responses and antagonizes IFN-? responses. Journal of Neuroimmunology. 200 (1-2): pp. 77-89.
    Source Title
    Journal of Neuroimmunology
    DOI
    10.1016/j.jneuroim.2008.06.013
    ISSN
    0165-5728
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/26942
    Collection
    • Curtin Research Publications
    Abstract

    A number of treatment options are available to multiple sclerosis patients, however this needs to be improved. Herein, we designed and synthesized a number of peptides by mutating principal TCR contact residues based on MBP83-99 peptide epitope. Immunization of SJL/J mice with MBP83-99 and mutant [A91]MBP83-99, [E91]MBP83-99, [F91]MBP83-99, [Y91]MBP83-99, and [R91, A96]MBP83-99 peptides, induced IFN-?, and only [R91, A96]MBP83-99 mutant peptide was able to induce IL-4 secretion by T cells. T cells against the native MBP83-99 peptide cross-reacted with all peptides except [Y91]MBP83-99 and [R91,A96]MBP83-99. The double mutant [R91, A96]MBP83-99 was able to antagonize IFN-? production in vitro by T cells against the native MBP83-99 peptide. Antibodies generated to [R91, A96]MBP83-99 did not cross-react with whole MBP protein. Molecular modeling between peptide analogs and H2 I-As demonstrated novel interactions. The [R91, A96]MBP83-99 double mutant peptide analog is the most promising for further therapeutic studies. © 2008 Elsevier B.V. All rights reserved.

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