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International Immunology, Vol. 15, No. 2, pp. 261-268, February 2003
© 2003 Japanese Society for Immunology

Encephalitogenic activity of truncated myelin oligodendrocyte glycoprotein (MOG) peptides and their recognition by CD8+ MOG-specific T cells on oligomeric MHC class I molecules

Deming Sun1,2, Yiping Zhang3, Bingyuan Wei4, Stephen C. Peiper2, Hui Shao1 and Henry J. Kaplan1

1 Kentucky Lions Eye Center, Department of Ophthalmology, and Vision Sciences, and 2 James Graham Brown Cancer Center, University of Louisville, Louisville, KY 40202, USA 3 Department of Neurology, University of California Irvine, Irvine, CA 92697-4275, USA 4 BD Biosciences PharMingen, San Diego, CA 92121, USA

Correspondence to: D. Sun, Kentucky Lions Eye Center, Department of Ophthalmology and Vision Sciences, University of Louisville, 301 E. Muhammad Ali Boulevard, Louisville, KY 40202, USA. E-mail: d0sun001{at}louisville.edu
Transmitting editor: L. Steinman

We have previously demonstrated that the 21-residue peptide pMOG35–55 from myelin oligodendrocyte glycoprotein (MOG) contains an antigenic epitope that activates CD8+ encephalitogenic T cells in C57BL/6 (B6) mice. To identify the core encephalitogenic epitope of CD8+ MOG-specific T cells, we have prepared a panel of highly purified peptides of varying lengths, which span the entire length of pMOG35–55, and tested their binding to recombinant H-2Db dimers and their ability to induce EAE. Two of the truncated peptides, pMOG40–54 and pMOG44–54, strongly bound recombinant H-2Db protein and this complex bound MOG-specific CD8+ T cells. Interestingly, pMOG40–54 retained the full capability of inducing paralytic disease, whereas only a part of the B6 mice immunized with pMOG44–54 developed clinical paralysis and central nervous system (CNS) inflammation. Further deletion of 1 amino acid from either the N- or C-terminus of the peptide pMOG44–54 dramatically reduced binding to recombinant H-2Db, and abolished the induction of paralysis and CNS inflammation. Our results demonstrate that the ability of truncated pMOG35–55 peptides to bind recombinant H-2Db protein does not always correlate with their ability of inducing encephalomyelitis. This approach enables the further identification of the core pathogenic epitope within the pMOG35–55 that activates MOG-specific encephalitogenic CD8+ T cells.

Keywords: CD8+ encephalitogenic T cell, epitope mapping, experimental autoimmune encephalomyelitis, myelin oligodendrocyte glycoprotein, tetramer


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