ArticlemAbs2019
Effects of terminal galactose residues in mannose α1-6 arm of Fc-glycan on the effector functions of therapeutic monoclonal antibodies.
Article in mAbs, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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Who cites it
44 citing papers in PubMed, 68 citations in OpenAlex.
- Selection of Functional Glycoforms in Anti-SARS-CoV-2 Human IgG1 Monoclonal Antibodies by FcγRIIIa Affinity Chromatography and Mass Spectrometry.Journal of medicinal chemistry · 2026Article
- Differences in mAb Galactosylation Caused by the Leaching of Manganese Ions from Different Bioreactors.Pharmaceutical research · 2026Article
- Immunoglobulin G N-glycosylation remodeling in viral infections: immunomodulatory roles and potential biomarker implications.Frontiers in immunology · 2026Review
- Glycoengineering of Monoclonal Antibodies with Homogeneous Glycan Isomers with Asymmetric Antennae.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A Surface Plasmon Resonance-Based Integrated Assay for Quantification and Glycosylation Characterization of Monoclonal Antibodies in Crude Heterogeneous Samples.Biotechnology and bioengineering · 2025Article
- A transposon-based transient transfection system in CHO-K1 cells enables quality prediction of stable cell line proteins.Bioprocess and biosystems engineering · 2025Article
- Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Temporal Galactose-Manganese Feeding in Fed-Batch and Perfusion Bioreactors Modulates UDP-Galactose Pools for Enhanced mAb Glycosylation Homogeneity.Biotechnology and bioengineering · 2025Article
- Characterization of Biosimilar Monoclonal Antibodies and Their Reference Products Approved in Japan to Reveal the Quality Characteristics in Post-approval Phase.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025Article
- Spotlight on Glycan Pairing: The Generation and Impact of Monoclonal Antibody Asymmetrical Fc N‑Glycan Pairs on Fc Receptor Interaction.ACS pharmacology & translational science · 2025Article
- Systematic Preparation of a 66-IgG Library with Symmetric and Asymmetric Homogeneous Glycans and Their Functional Evaluation.Journal of the American Chemical Society · 2024Article
- Glycosylation: mechanisms, biological functions and clinical implications.Signal transduction and targeted therapy · 2024Review
- GlYcoLISA: antigen-specific and subclass-specific IgG Fc glycosylation analysis based on an immunosorbent assay with an LC-MS readout.Nature protocols · 2024Review
- Functional prediction of the potential NGLY1 mutations associated with rare disease CDG.Heliyon · 2024Article
- Comparison of N-Glycopeptide to Released N-Glycan Abundances and the Influence of Glycopeptide Mass and Charge States on N-Linked Glycosylation of IgG Antibodies.Journal of proteome research · 2024Article
- Transcriptomics as a predictor of biopharmaceutically favourable glycan profiles.Frontiers in cell and developmental biology · 2024Article
- Glycosylation shapes the efficacy and safety of diverse protein, gene and cell therapies.Biotechnology advances · 2023Review
- Optimizing effector functions of monoclonal antibodies via tailored N-glycan engineering using a dual landing pad CHO targeted integration platform.Scientific reports · 2023Article
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Constant domain polymorphisms influence monoclonal antibody stability and dynamics.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation). Terminal galactose (Gal) residues of Fc-glycans are known to influence effector functions such as antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity (CDC), but the impact of the G1F isomers (G1aF and G1bF) on the effector functions has not been reported. Here, we prepared four types of glycoengineered anti-CD20 mAbs bearing homogeneous G2F, G1aF, G1bF, or G0F (G2F mAb, G1aF mAb, G1bF mAb, or G0F mAb, respectively), and evaluated their biological activities. Interestingly, G1aF mAb showed higher C1q- and FcγR-binding activities, CDC activity, and FcγR-activation property than G1bF mAb. The activities of G1aF mAb and G1bF mAb were at the same level as G2F mAb and G0F mAb, respectively. Hydrogen-deuterium exchange/mass spectrometry analysis of dynamic structures of mAbs revealed the greater involvement of the terminal Gal residue on the Man α1-6 arm in the structural stability of the CH2 domain. Considering that mAbs interact with FcγR and C1q via their hinge proximal region in the CH2 domain, the structural stabilization of the CH2 domain by the terminal Gal residue on the Man α1-6 arm of Fc-glycans may be important for the effector functions of mAbs. To our knowledge, this is the first report showing the impact of G1F isomers on the effector functions and dynamic structure of mAbs.
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