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We have previously demonstrated that the 21‐residue peptide pMOG_35–55 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 pMOG_35–55, and tested their binding to recombinant H‐2D^b dimers and their ability to induce EAE. Two of the truncated peptides, pMOG_40–54 and pMOG_44–54, strongly bound recombinant H‐2D^b protein and this complex bound MOG‐specific CD8⁺ T cells. Interestingly, pMOG_40–54 retained the full capability of inducing paralytic disease, whereas only a part of the B6 mice immunized with pMOG_44–54 developed clinical paralysis and central nervous system (CNS) inflammation. Further deletion of 1 amino …