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Immunomodulation of Experimental Autoimmune Encephalomyelitis with Ordered Peptides Based on MHC-TCR Binding Motifs¹

Pedro J. Ruiz^2,3,*, Jason J. DeVoss^2,*, Louis-Vu T. Nguyen^*, Paulo P. Fontoura^*, David L. Hirschberg^*, Dennis J. Mitchell^*, K. Christopher Garcia and Lawrence Steinman^*

Departments of ^* Neurology and Neurological Sciences and Structural Biology, Stanford University School of Medicine, Stanford, CA 94305

T cell-mediated destruction of the myelin sheath causes inflammatory damage of the CNS in multiple sclerosis (MS). The major T and B cell responses in MS patients who are HLA-DR2 (about two-thirds of MS patients) react to a region between residues 84 and 103 of myelin basic protein (1 ). The crystal structure of HLA-DR2 complexed with myelin basic protein_84–102 confirmed that Lys⁹¹ is the major TCR contact site, whereas Phe⁹⁰ is a major anchor to MHC and binds the hydrophobic P4 pocket (2 ). We have tested peptides containing repetitive 4-aa sequences designed to bind critical MHC pockets and to interfere with T cell activation. One such sequence, EYYKEYYKEYYK, ameliorates experimental autoimmune encephalomyelitis in Lewis rats, an animal model of MS.

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