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dc.contributor.authorKatsara, M.
dc.contributor.authorYuriev, E.
dc.contributor.authorRamsland, Paul
dc.contributor.authorDeraos, G.
dc.contributor.authorTselios, T.
dc.contributor.authorMatsoukas, J.
dc.contributor.authorApostolopoulos, V.
dc.identifier.citationKatsara, 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.

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.

dc.publisherElsevier BV
dc.titleA double mutation of MBP83-99 peptide induces IL-4 responses and antagonizes IFN-? responses
dc.typeJournal Article
dcterms.source.titleJournal of Neuroimmunology
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available

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