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

Maria Katsara, Elizabeth Yuriev, Paul Allen Ramsland, George Deraos, Theodore Tselios, John Matsoukas, Vasso Apostolopoulos

Research output: Contribution to journalArticleResearchpeer-review

24 Citations (Scopus)

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 [(YMBP83-99)-M-91] 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-A(s). Molecular modeling was used to identify H-bonding and van der Waals interactions between peptides and MHC (I-A(s)). (C) 2008 Elsevier Ltd. All rights reserved
Original languageEnglish
Pages (from-to)3661 - 3670
Number of pages10
JournalMolecular Immunology
Volume45
Issue number13
Publication statusPublished - 2008

Cite this

Katsara, M., Yuriev, E., Ramsland, P. A., Deraos, G., Tselios, T., Matsoukas, J., & Apostolopoulos, V. (2008). Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2. Molecular Immunology, 45(13), 3661 - 3670.
Katsara, Maria ; Yuriev, Elizabeth ; Ramsland, Paul Allen ; Deraos, George ; Tselios, Theodore ; Matsoukas, John ; Apostolopoulos, Vasso. / Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2. In: Molecular Immunology. 2008 ; Vol. 45, No. 13. pp. 3661 - 3670.
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title = "Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2",
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 [(YMBP83-99)-M-91] 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-A(s). Molecular modeling was used to identify H-bonding and van der Waals interactions between peptides and MHC (I-A(s)). (C) 2008 Elsevier Ltd. All rights reserved",
author = "Maria Katsara and Elizabeth Yuriev and Ramsland, {Paul Allen} and George Deraos and Theodore Tselios and John Matsoukas and Vasso Apostolopoulos",
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Katsara, M, Yuriev, E, Ramsland, PA, Deraos, G, Tselios, T, Matsoukas, J & Apostolopoulos, V 2008, 'Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2', Molecular Immunology, vol. 45, no. 13, pp. 3661 - 3670.

Mannosylation of mutated MBP83-99 peptides diverts immune responses from Th1 to Th2. / Katsara, Maria; Yuriev, Elizabeth; Ramsland, Paul Allen; Deraos, George; Tselios, Theodore; Matsoukas, John; Apostolopoulos, Vasso.

In: Molecular Immunology, Vol. 45, No. 13, 2008, p. 3661 - 3670.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Katsara, Maria

AU - Yuriev, Elizabeth

AU - Ramsland, Paul Allen

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AU - Tselios, Theodore

AU - Matsoukas, John

AU - Apostolopoulos, Vasso

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AB - 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 [(YMBP83-99)-M-91] 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-A(s). Molecular modeling was used to identify H-bonding and van der Waals interactions between peptides and MHC (I-A(s)). (C) 2008 Elsevier Ltd. All rights reserved

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