Background: Myelin oligodendrocyte glycoprotein (MOG) is located on the external surface
of myelin, a membranous component of the central nervous system (CNS) that forms the insulating
lipid layer around neurons. The major MOG splicing variant (a1 transcript) encodes a transmembrane
protein with an extracellular domain of an Ig variable (IgV) fold. MOG IgV domains from the
same or different cells dimerize and contribute to the organization and maintenance of the myelin
sheath in neurons. The encepalitogenic T cells recognize MOG and its immunodominant epitopes (epitopes
1-22, 35-55 and 92-106 located at the dimer interface) as foreign antigens and cause the destruction
of myelin (demyelination) leading to the clinical condition known as multiple sclerosis (MS).
Recognition of the antigen takes place in the context of the trimolecular complex formed by HLA,
MOGpeptides and TCR.
Objective: Understanding the role of MOG in MS.
Method/Results: We have reviewed herein, the genomic organization of the human MOG gene, the
structural characteristics of the MOG protein, the involvement of MOG in MS and clinical studies for
the treatment of MS based on MOG peptide analogues.
Conclusion: Conjugates of antigenic MOG peptides to mannan and combinations of antigenic MOG
and other peptides chemically linked to cells of the immune system may modify the immune response,
alleviating in some cases the symptoms of MS.