CD Evidence of the Conformational Transitions in rMOG[1–125] in the Presence of Membrane Mimicking Detergents

Abstract

Myelin oligodendrocyte glycoprotein (MOG), an integral glycoprotein associated with the myelin in brain nerve fibers, has recently been implicated as a prime autoantigen leading to autoimmune demyelination in animal models (experimental autoimmune encephalomyelitis, EAE). Immunization of animal models, including mice and marmosets, with rMOG led to the manifestation of a disease similar to multiple sclerosis (MS) — demyelination mediated by autoantibodies directed against the extracellular domain of MOG (MOG[1-125]) [1]. The extracellular location of MOG has been identified as a member of the immunoglobulin superfamily by Gardinier et al. [2]. The amino acid sequence of rat MOG[1-125] (139 residues) is as follows; MRGS-FRVIGPGHPIRALVGDEAELPCRISPGKNATGMEVGWYRSPFSRVVHL YRNGKDQDAEQAPEYRGRTELLKESIGEGKVALRIQNVRFSDEGGYTCFFRDH SYQEEAAVELKVEDPFYWINPG-RSQSHHHHHH.