Myelin Oligodendrocyte Glycoprotein Gene

Publisher Summary Myelin oligodendrocyte glycoprotein (MOG) is a protein of great neuroimmunological interest, whose function is not known. This chapter examines the structural functional relationships of MOG in myelin. Two different strategies are used to clone MOG mRNAs. One uses a mixture of MOG mAbs to screen a rat ƛgt11 expression library, whereas other used degenerate primers developed from the N-terminal amino acid sequence of bovine MOG to screen bovine, rat, and mouse brain ƛgt10 phage libraries. Subsequently, the mouse gene is isolated and its organization characterized. Similar approaches are used to characterize the human MOG cDNA and the human gene. Sequence analyses indicate that the mature protein is highly conserved between species and consists of 218 amino acids comprising a putative signal peptide, an immunoglobulin (Ig)-like N-terminal domain, two highly hydrophobic segments separated by a short hydrophilic loop, and a short hydrophilic C-terminal domain. The presence of two putative membrane-spanning domains, if verified, would make MOG a unique member of the Ig super-gene family (IgSF).