The role of N-glycan in folding, trafficking and pathogenicity of myelin oligodendrocyte glycoprotein (MOG)

Abstract

Myelin oligodendrocyte glycoprotein (MOG) is a type I integral membrane protein that is expressed in the central nervous system. MOG has a single N-glycosylation site within its extracellular domain. MOG has been linked with pathogenesis of multiple sclerosis; anti-MOG antibodies have been detected in the sera of multiple sclerosis patients. N-glycosylation is an important post-translational modification of protein that might impact their folding, localization and function. However, the role of sugar in the biology of MOG is not well understood. In this study, we created a mutant MOG lacking N-linked glycan and tested its properties. We concluded that the lack of sugar did not impact on MOG abundance in the absence of endoplasmic reticulum molecular chaperone calnexin. We also show that the absence of N-glycan did not interfere with MOG's subcellular localization and it did not result in activation of endoplasmic reticulum stress. This article is part of a Special Issue entitled: 13th European Symposium on Calcium.

Keywords: Calnexin; Calreticulin; ERp57; Endoplasmic reticulum; Molecular chaperones; Myelin oligodendrocyte glycoprotein (MOG).