Altered Glycosylation of Subclass IgG1 Recombinant Human Immunoglobulin by Selecting Culture Conditions for Producers and Additives

The possibility to alter the glycosylation profile is an important prerequisite for the development of production technologies of therapeutic recombinant immunoglobulins. Glycans affect various effector functions of the antibody, such as antibody-dependent cell-mediated cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and the drug half-life. The possibility to achieve the required glycosylation profile of a therapeutic antibody by optimizing cultivation conditions will facilitate both the creation of more effective drugs and accelerated development of biosimilars. The conducted study found that an increase in the cultivation duration leads to a decrease in the galactose content. The addition of the EM-N-glycan regulator-2 afucose regulator (Eminence, China) led to an increase in the content of afucosylated glycans. The co-expression of the Fut8 enzyme led to an increase in mannose residues. Various approaches to regulation of fucose, mannose, and galactose contents during biosynthesis of IgG1 therapeutic antibody were tested.