Glycan Remodeling of Glycoproteins Using ENGases

Abstract

Recently, homogenous glycoprotein has been prepared by using a chemoenzymatic approach to investigate the function of glycoproteins. Glycoproteins produced by cultured cells generally have heterogeneous glycans, so it is unclear which glycan is associated with the function of the glycoprotein. Moreover, because glycoproteins are heterogeneous, it is difficult to analyze their structure by X-ray crystal diffraction or NMR measurement. To solve this problem, transgenic cells have been developed to produce homogeneous glycoproteins through control of the biosynthetic pathway, but it is difficult to prepare glycoproteins with various kinds of homogeneous glycan by using this approach. Therefore, a chemoenzymatic approach using ENGase has been developed, and it enables the replacement of various glycans. Because antibody-dependent cell-mediated cytotoxicity (ADCC) exists as an example of glycan function in glycoproteins, there have been many studies of glycan remodeling of antibodies. Here, I introduce recent research and technologies, and their progress, in the field of glycan remodeling.

Preparation of <i>N</i>-Glycans from Natural Products

“…It has been reported that many kinds of N-glycans can be prepared from the hen egg-derived glycan using chemical or enzymatic methods (12)(13)(14)(15)(16)(17). There are many reports on the synthesis of glycoproteins and glycopeptides using complex and high-mannose-type sugar chains obtained from natural products such as chicken eggs and soybeans (18)(19)(20).…”