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• W2013264850 endingPage "12318" @default.
• W2013264850 startingPage "12308" @default.
• W2013264850 abstract "The fine structures of Fc N-glycans can modulate the effector functions of IgG antibodies. It has been demonstrated that lack of the core fucose on the Fc N-glycans leads to drastic enhancement of antibody-dependent cellular cytotoxicity (ADCC), while terminal α2,6-sialylation of Fc glycan plays a critical role for the anti-inflammatory activity of human intravenous immunoglobulin (IVIG). We describe in this paper a highly efficient chemoenzymatic method for site-selective Fc glycoengineering of intact monoclonal antibody and IVIG. Two new glycosynthase mutants (EndoS-D233A and D233Q) were generated by site-directed mutagenesis of EndoS (an endoglycosidase from Streptococcus pyogenes) and were found to be capable of efficiently transferring predefined N-glycans from corresponding glycan oxazolines to the Fc-deglycosylated intact IgGs without product hydrolysis. As a model study, rituximab (a therapeutic monoclonal antibody) was successfully transformed from mixtures of G0F, G1F, and G2F glycoforms to well-defined homogeneous glycoforms, including a fully sialylated (S2G2F) glycoform that may gain anti-inflammatory activity, a nonfucosylated G2 glycoform that showed significantly enhanced FcγIIIa receptor-binding activity, and an azido-tagged glycoform that can be further transformed into other glycoforms. We also found that EndoS could selectively remove the Fc N-glycans in the presence of FAB glycosylation. This finding, coupled with the remarkable transglycosylation activity of the EndoS glycosynthase mutants, permitted a highly selective glycoengineering of the IVIG’s Fc glycans into a fully sialylated Fc glycoform, which may possess significantly enhanced anti-inflammatory activity. The glycoengineering approach described here provides a general platform to modulate the effector functions of IgG antibodies, enabling the optimization of therapeutic efficacy and gain of new functions of monoclonal antibodies and IVIG." @default.
• W2013264850 created "2016-06-24" @default.
• W2013264850 creator A5036627086 @default.
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• W2013264850 creator A5064042195 @default.
• W2013264850 creator A5077552203 @default.
• W2013264850 date "2012-07-16" @default.
• W2013264850 modified "2023-10-10" @default.
• W2013264850 title "Chemoenzymatic Glycoengineering of Intact IgG Antibodies for Gain of Functions" @default.
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• W2013264850 doi "https://doi.org/10.1021/ja3051266" @default.
• W2013264850 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3427744" @default.
• W2013264850 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22747414" @default.
• W2013264850 hasPublicationYear "2012" @default.
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