It has been well-documented that the terminal sugars of Fc glycans can play a critical role in the safety and efficacy of therapeutic monoclonal antibodies (mAbs). However, many of the effects of highly heterogeneous Fc glycan structures have yet to be fully characterized. Different glycosylation patterns can affect Fcdependent activities such as the ability of mAbs to bind Fcγ receptors (FcγRs) on the effector cell surface, which is critical to immune effector functions such as antibody dependent cellular cytotoxicity (ADCC).Previous studies on the impact of sialic acid in the Fc glycan on ADCC has not resulted in consistent conclusions. In our study we tested sialic acid enriched species from a chimeric murine/human kappa light chain IgG1 (mAb1) with known FcγRIIIa binding and ADCC activities. These enriched species contained up to a four-fold increase in sialic acid-containing glycans relative to the typical levels present in therapeutic mAbs, along with other attributes such as oxidized and deamidated species. The ADCC analysis of sialylated
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