ArticleScientific reports2018
Assessing the Heterogeneity of the Fc-Glycan of a Therapeutic Antibody Using an engineered FcγReceptor IIIa-Immobilized Column.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Molecular Basis of Core Fucosylation-Dependent Modulation of IgG1 Fc-CD16a Binding.bioRxiv : the preprint server for biology · 2026Article
- Mitigating alkaline instability induced by tyrosine-tyrosine repulsion in an FcγRIIIa-binding protein through phenylalanine substitution.Journal of biochemistry · 2026Article
- 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
- Antibody therapeutics with high affinity for FcγRs exacerbate anaphylaxis via FcγR-mediated capture by tumor-associated myeloid cells.Journal for immunotherapy of cancer · 2026Article
- Development of tCAP(N3): Affinity Peptide-Aided, pH-Triggered Strategy for Site-Specific Native IgG Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026Review
- 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
- Optimized expression of human interleukin-15 inBiotechnology reports (Amsterdam, Netherlands) · 2025Article
- Current advances in separation chemistry for antibody purification and analysis.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025Review
- Systematic Preparation of a 66-IgG Library with Symmetric and Asymmetric Homogeneous Glycans and Their Functional Evaluation.Journal of the American Chemical Society · 2024Article
- The expression system affects the binding affinity between p75NTR and proNGF.Biochemistry and biophysics reports · 2024Article
- Specific peptide conjugation to a therapeutic antibody leads to enhanced therapeutic potency and thermal stability by reduced Fc dynamics.Scientific reports · 2023Article
- Article
- Chromatographic Analysis of theACS omega · 2023Article
- Biophysical Characterization of the Contribution of the Fab Region to the IgG-FcγRIIIa Interaction.Biochemistry · 2023Article
- Production andFrontiers in plant science · 2023Article
- Negative interference with antibody-dependent cellular cytotoxicity mediated by rituximab from its interactions with human serum proteins.Frontiers in immunology · 2023Article
- Characterization of FcγRIa (CD64) as a Ligand Molecule for Site-Specific IgG1 Capture: A Side-By-Side Comparison with Protein A.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Afucosylated IgG responses in humans - structural clues to the regulation of humoral immunity.Trends in immunology · 2022Review
- Alteration of rhesus macaque serum N-glycome during infection with the human parasitic filarial nematode Brugia malayi.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-glycan moiety of IgG-Fc has a significant impact on multifaceted properties of antibodies such as in their effector function, structure, and stability. Numerous studies have been devoted to understanding its biological effect since the exact composition of the Fc N-glycan modulates the magnitude of effector functions such as the antibody-dependent cell mediated cytotoxicity (ADCC), and the complement-dependent cytotoxicity (CDC). To date, systematic analyses of the properties and influence of glycan variants have been of great interest. Understanding the principles on how N-glycosylation modulates those properties is important for the molecular design, manufacturing, process optimization, and quality control of therapeutic antibodies. In this study, we have separated a model therapeutic antibody into three fractions according to the composition of the N-glycan by using a novel FcγRIIIa chromatography column. Notably, Fc galactosylation was a major factor influencing the affinity of IgG-Fc to the FcγRIIIa immobilized on the column. Each antibody fraction was employed for structural, biological, and physicochemical analysis, illustrating the mechanism by which galactose modulates the affinity to FcγRIIIa. In addition, we discuss the benefits of the FcγRIIIa chromatography column to assess the heterogeneity of the N-glycan.
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