CD BioGlyco has established high-quality Platforms for glycobiology research. We provide clients with professional and efficient glycoengineering services, such as glyco-engineered systems for glycoprotein expression, protein glycoengineering, and antibody glycoengineering.
Almost all therapeutic proteins are glycosylated. The clinical efficacy and safety of therapeutic glycoproteins are influenced by the distribution, structure, and composition of their glycosyl groups. Glycoengineering is a method of improving protein properties by changing glycosylation. Specifically, glycoengineering is performed by changing the number and location of glycosylation sites or by changing the glycan structure of individual glycosylation sites. Glycoengineering is divided into two categories according to the produced way of glycoproteins: cell-based glycoengineering and chemical-based glycoengineering. Here, we will describe these two classes of glycoengineering in detail.
Mammalian cells, especially Chinese hamster ovary (CHO) cells, have been widely used for the production of therapeutic glycoproteins. One glycoengineering strategy is to change the structure of glycans on proteins in CHO cells by knocking out genes. For example, Knockout of α-1,6-fucosyltransferase (FUT8) in CHO cells to produce therapeutic immunoglobulin (IgG) antibodies with enhanced antibody-dependent cell-mediated cytotoxicity (ADCC). There is also a glycoengineering strategy to improve the efficacy of therapeutic glycoproteins by changing the number of glycosylation sites. For example, the introduction of a new N-glycosylation site into human erythropoietin (hEPO) increases its clinical efficacy. In addition, many other cell types have been reported for protein glycoengineering, such as plant cells, insect cells, yeast cells, and bacterial cells.
Fig.1 Cell-based glycoengineering. (Jaroentomeechai, et al., 2020)
Chemical-based glycoengineering strategies are mainly catalyzed by glycosidase or glycosyltransferase to generate glycosidic bonds or cleavage of glycosidic bonds. For example, the efficacy of IgG is enhanced by changing the glycosidic linkage between the terminal sialic acid residue and the penultimate galactose residue. This strategy readily produces homogeneous proteins.
Fig.2 Endoglycosynthase (ENGases)-mediated preparation of homogeneous N-glycoproteins. (Jaroentomeechai, et al., 2020)
CD BioGlyco provides efficient and stable mammalian cell, Pichia pastoris, and plant-based glycoengineered expression systems for global clients to produce homogeneous glycoproteins.
We have established an advanced IVGE platform. Our strategy is to modify glycoproteins by altering the number and location of glycosylation sites or altering the glycan structure of individual glycosylation sites.
CD BioGyco has developed many genefic strategies to manipulate glycosylation to further meet the special needs of glycosylation in biopharmaceutical, disease research, and other fields.
CD BioGlyco has extensive expertise in the field of glycoengineering. We not only provide our clients with glycoengineered expression systems based on mammalian, Pichia pastoris, and plant cells, but also provide custom cell lines for each specific need. Our chemical-based in vitro glycoengineering is used to produce glycoproteins with well-defined and uniform Fc glycoforms, resulting in improved biopharmaceutical safety, consistency, and reduced immunogenicity. We also provide sialic acid glycoengineering service, which introduces unnatural sialic acids of different chemical properties into sialic glycans.
CD BioGlyco is a leading service provider specializing in the efficient glycoengineering platform. If you are interested in our glycoengineering platform, please contact us for more information.
CD BioGlyco is a world-class biotechnology company with offices in many countries. Our products and services provide a viable option to what is otherwise available.