Characterization of MHC- and TCR-binding residues of the myelin oligodendrocyte glycoprotein 38-51 peptide.

摘要: Myelin oligodendrocyte glycoprotein (MOG) is a major experimental autoimmune encephalomyelitis (EAE) antigen in H-2b mice and potential autoantigen multiple sclerosis. How well MOG peptides bind to MHC how TCR recognize the peptide/MHC complex have important implications for thymic selection as T cell activation periphery. In this study, we characterized amino acids MOG(38-51) peptide binding I-Ab, recognition of complex. We found that R41, F44, R46 V47 constituted contact residues, alanine substitution at these positions abrogated responses without decreasing their affinity I-Ab. addition, G38 W39 were be minor residues. Finally, substituting tyrosine position 40 decreased I-Ab by approximately 50% prevented induction C57BL/6J upon immunization. Thus, Y40 dominant MHC-binding residue most likely occupies p1 pocket Our results could useful design with altered agretopes epitopes study therapeutic EAE model.