Myelin oligodendrocyte glycoprotein (MOG), extracellular Ig-like domain (MOG)

Myelin oligodendrocyte glycoprotein (MOG) is a transmembrane protein belonging to the immunoglobulin superfamily, specifically localized to the outermost surface of myelin sheaths and oligodendrocyte membranes in the central nervous system (CNS) [UniProt: P47865]. The extracellular Ig-like domain of MOG is highly immunogenic and serves as a critical target for autoantibodies in various demyelinating diseases, most notably MOG antibody-associated disease (MOGAD) and some forms of multiple sclerosis [PubMed: 32773315]. While its exact physiological role is not fully understood, it is believed to function as a cell surface receptor or adhesion molecule involved in the completion and maintenance of the myelin sheath and the regulation of oligodendrocyte microtubule stability [NCBI Gene: 4340]. In pathological states, the binding of IgG autoantibodies to the extracellular domain triggers complement-dependent cytotoxicity and antibody-dependent cellular cytotoxicity, leading to myelin damage [PubMed: 29604560]. Therapeutic strategies currently under investigation focus on inducing antigen-specific immune tolerance to MOG, such as through the use of glycosylated MOG peptides or tolerogenic dendritic cells, to prevent the autoimmune destruction of CNS tissue [ClinicalTrials.gov: NCT04602286]. This approach aims to provide a more targeted treatment compared to broad immunosuppression, potentially reducing side effects while maintaining CNS integrity. Monitoring anti-MOG antibody titers serves as a critical biomarker for diagnosis and treatment response in clinical practice [PubMed: 30396544].

Other names

MOGMyelin-oligodendrocyte glycoproteinMOGAD antigenMOG Ig-like domain

Antigen-specific immune tolerance induction