ArticlePloS one2015
Glycoengineered Monoclonal Antibodies with Homogeneous Glycan (M3, G0, G2, and A2) Using a Chemoenzymatic Approach Have Different Affinities for FcγRIIIa and Variable Antibody-Dependent Cellular Cytotoxicity Activities.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 94 citations in OpenAlex.
- Glycoengineering of Monoclonal Antibodies with Homogeneous Glycan Isomers with Asymmetric Antennae.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Robust and Reproducible Monoclonal Antibody Production Using a Transgenic Silkworm System.International journal of molecular sciences · 2025Article
- Discovery of a single-subunit oligosaccharyltransferase that enables glycosylation of full-length IgG antibodies in bacteria.Nature communications · 2025Article
- Highly variable aggregation and glycosylation profiles and their roles in immunogenicity to protein-based therapeutics.Journal of pharmaceutical sciences · 2025Review
- ADCC: the rock band led by therapeutic antibodies, tumor and immune cells.Frontiers in immunology · 2025Review
- Direct glycosylation analysis of intact monoclonal antibodies combining ESI MS of glycoforms and MALDI-in source decay MS of glycan fragments.Communications chemistry · 2024Article
- Systematic Preparation of a 66-IgG Library with Symmetric and Asymmetric Homogeneous Glycans and Their Functional Evaluation.Journal of the American Chemical Society · 2024Article
- Article
- Study on antibody Fc-glycosylation for optimal effector functions.Chemical communications (Cambridge, England) · 2023Article
- Glycoconjugates: Synthesis, Functional Studies, and Therapeutic Developments.Chemical reviews · 2022Review
- Synthesis of glycopeptides and glycopeptide conjugates.Organic & biomolecular chemistry · 2022Review
- Strategies to control therapeutic antibody glycosylation during bioprocessing: Synthesis and separation.Biotechnology and bioengineering · 2022Review
- Production of galactosylated complex-type N-glycans in glycoengineered Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2022Article
- Structural insight and stability of TNFR-Fc fusion protein (Etanercept) produced by using transgenic silkworms.Journal of biochemistry · 2021Article
- Importance and Monitoring of Therapeutic Immunoglobulin G Glycosylation.Experientia supplementum (2012) · 2021Review
- Innovative Preparation of Biopharmaceuticals Using Transglycosylation Activity of Microbial Endoglycosidases.Journal of applied glycoscience · 2021Article
- Impact of IgG1 N-glycosylation on their interaction with Fc gamma receptors.Current research in immunology · 2020Article
- Principles ofAntibodies (Basel, Switzerland) · 2020Review
- Enhancement of sialylation in rIgG in glyco-engineered Chinese hamster ovary cells.Cytotechnology · 2020Article
- Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells.Frontiers in chemistry · 2020Review
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many therapeutic antibodies have been developed, and IgG antibodies have been extensively generated in various cell expression systems. IgG antibodies contain N-glycans at the constant region of the heavy chain (Fc domain), and their N-glycosylation patterns differ during various processes or among cell expression systems. The Fc N-glycan can modulate the effector functions of IgG antibodies, such as antibody-dependent cellular cytotoxicity (ADCC) and complement dependent cytotoxicity (CDC). To control Fc N-glycans, we performed a rearrangement of Fc N-glycans from a heterogeneous N-glycosylation pattern to homogeneous N-glycans using chemoenzymatic approaches with two types of endo-β-N-acetyl glucosaminidases (ENG'ases), one that works as a hydrolase to cleave all heterogeneous N-glycans, another that is used as a glycosynthase to generate homogeneous N-glycans. As starting materials, we used an anti-Her2 antibody produced in transgenic silkworm cocoon, which consists of non-fucosylated pauci-mannose type (Man2-3GlcNAc2), high-mannose type (Man4-9GlcNAc2), and complex type (Man3GlcNAc3-4) N-glycans. As a result of the cleavage of several ENG'ases (endoS, endoM, endoD, endoH, and endoLL), the heterogeneous glycans on antibodies were fully transformed into homogeneous-GlcNAc by a combination of endoS, endoD, and endoLL. Next, the desired N-glycans (M3; Man3GlcNAc1, G0; GlcNAc2Man3GlcNAc1, G2; Gal2GlcNAc2Man3GlcNAc1, A2; NeuAc2Gal2GlcNAc2Man3GlcNAc1) were transferred from the corresponding oxazolines to the GlcNAc residue on the intact anti-Her2 antibody with an ENG'ase mutant (endoS-D233Q), and the glycoengineered anti-Her2 antibody was obtained. The binding assay of anti-Her2 antibody with homogenous N-glycans with FcγRIIIa-V158 showed that the glycoform influenced the affinity for FcγRIIIa-V158. In addition, the ADCC assay for the glycoengineered anti-Her2 antibody (mAb-M3, mAb-G0, mAb-G2, and mAb-A2) was performed using SKBR-3 and BT-474 as target cells, and revealed that the glycoform influenced ADCC activity.
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