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Myelin basic protein (MBP), myelin oligodendrocyte glycoprotein (MOG), and proteolipid protein (PLP) are the primary structural proteins of the central nervous system (CNS) myelin sheath and serve as the major autoantigens in multiple sclerosis (MS) [1, 9]. In MS, the immune system's tolerance to these proteins is lost, leading to the activation of autoreactive T cells that recognize specific antigenic peptides (epitopes) presented by MHC molecules [10, 11]. This recognition triggers an inflammatory cascade that results in demyelination, axonal loss, and progressive neurological disability [1, 13]. Therapeutic strategies targeting these peptides, such as antigen-specific immunotherapy and tolerogenic vaccines, aim to selectively silence the autoimmune response by inducing T-cell anergy or promoting the expansion of regulatory T cells (Tregs) [4, 6]. Drugs like glatiramer acetate act as altered peptide ligands to divert the immune response, while experimental therapies like ATX-MS-1467 utilize specific MBP peptide sequences to restore long-term immune tolerance [3, 4]. Despite their potential for high specificity and reduced side effects compared to broad immunosuppressants, these therapies face challenges including the risk of disease exacerbation and the need for precise patient stratification based on HLA genotypes [2, 13].
Induction of antigen-specific immune tolerance, T-cell anergy, and expansion of regulatory T cells (Tregs) to suppress autoimmune attacks on the myelin sheath.
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