CD BioGlyco provides an integrated solution of glycoengineered antibody-based glycomedicine development. Our advanced technology platforms and high-quality services will fully meet your needs. We have the confidence to be your essential research assistant in the field of glycobiology.
Antibodies, also known as immunoglobulins, play essential roles in the immune system. They are used by the immune system to fight against invasive pathogens through direct neutralization, by activation of the complement system for cell lysis, and/or by facilitating phagocytosis of pathogens. Antibodies, as represented by IgG-type monoclonal antibodies (mAbs), are an important class of therapeutic proteins widely used for the treatment of cancer and autoimmune diseases. IgG is also the most abundant isotype of antibodies in blood circulation, accounting for approximately 75% of human immunoglobulins. A typical IgG antibody is composed of two light and two heavy chains that are associated to form three protein domains: two identical Fab regions specific for antigen binding and an Fc domain (constant or crystallizable IgG fragment) responsible for engaging various Fc receptors in antibody effector functions. The Fab domain and the Fc domain are connected by a flexible hinge region. The IgG-Fc domain is a homodimer, in which the two third constant domains (CH3 domains) are paired through noncovalent interactions, while each of the two second constant domains (CH2 domains) carries an N-linked oligosaccharide at the conserved N-glycosylation site.
Ample experimental data have shown that glycosylation can profoundly affect the biological functions and therapeutic efficacy of antibodies. Moreover, recent studies have further demonstrated that the fine structures of glycans, particularly those attached to the Fc domain, can differentially tune the immunological properties of a given antibody. These studies showcase the significance of antibody glycosylation for biological function.
Fig.1 Structures of a typical IgG antibody and the Fc N-glycans. (Huang, et al.2012)
Natural and recombinant antibodies are usually produced as heterogeneous mixtures of glycoforms that are extremely difficult to separate or enrich to isolate pure forms. Thus, methods that can lead to the production of structurally well-defined homogeneous glycoforms of antibodies are needed for both functional studies and the development of more efficient antibody-based therapeutics. Several aspects of antibody glycosylation have been explored to control and modulate the glycosylation pattern of antibodies. One is the genetic approach that focuses on controlling protein glycosylation by manipulating the N-glycan biosynthetic pathways in different host expression systems. Another promising strategy is in vitro glycan remodeling via chemoenzymatic synthesis which could lead to highly homogeneous antibody glycoforms. In addition, glycoengineering of Fc N-glycans is emerging as an attractive method for site-specific antibody-drug conjugation. CD BioGlyco provides high-quality services in these three major areas of glycoengineering of antibodies.
With a first-class carbohydrate-based glycomedicine development platform and professional research teams, CD BioGlyco is committed to ensuring that every service provides the highest level of satisfaction. Our professional research teams provide customers with high-quality glycoengineered antibody-based glycomedicine development services according to their needs. If you are interested in our services, please contact us to obtain more information.