CHO Pharma, Inc.

In the original publication, there is an error in figure 3; the correction is provided here.

Antibodies have been developed as therapeutic agents for the treatment of cancer, infection, and inflammation. In addition to binding activity toward the target, IgG antibodies also modulate the effector functions through the interaction of the fine structures of Fc N-glycans and the Fc receptors on immune cells. It has been demonstrated that antibodies lacking core fucosylation show a large increase in affinity for FcγRIIIa leading to an improved receptor-mediated effector function, antibody-mediated cellular cytotoxicity (ADCC). Terminal alpha-2,6-sialylation of Fc glycan was speculated to plays a critical role for the anti-inflammatory activity of human i.v. Ig (IVIG). To identify the optimal glycan structures for individual antibodies with desired activity, we have developed an effective method using new glycosynthase mutants to efficiently transfer predefined N-glycans oxazolines to the Fc-deglycosylated intact IgGs to furnish a homogeneous glycoform. In this study, we found that the biantennary N-glycan structure with two terminal alpha-2,6-linked sialic acids is a common and optimized structure for the enhancement of antibody-dependent cell-mediated cytotoxicity, complement-dependent cytotoxicity (CDC), and anti-inflammatory activities.