ArticleACS chemical biology2018
Antibody Fucosylation Lowers the FcγRIIIa/CD16a Affinity by Limiting the Conformations Sampled by the N162-Glycan.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 91 citations in OpenAlex.
- Afucosylated VAR2CSA-Specific IgG Reduces Risks of Placental Malaria.The Journal of infectious diseases · 2026Article
- Molecular Basis of Core Fucosylation-Dependent Modulation of IgG1 Fc-CD16a Binding.bioRxiv : the preprint server for biology · 2026Article
- Aglycosylated Immunoglobulin G1 Fc Stabilized Through Disulfide Bond Addition Exhibits Compositional Homogeneity and Retains Fc γ Receptor IIIa/CD16a Binding.Antibodies (Basel, Switzerland) · 2026Article
- Mouse Fc-FcγRIV structure guides Fc engineering for cross-species FcγR recognition.bioRxiv : the preprint server for biology · 2026Article
- The impact of N-glycan conformational entropy on the binding affinity of Fc γ receptor IIIa/CD16a.Structure (London, England : 1993) · 2026Article
- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
- Microsecond Dynamics of Fc-CD16a Recognition: Impact of Mutations, Core Fucosylation, and Fc Asymmetry.Antibodies (Basel, Switzerland) · 2026Article
- Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease.Nature communications · 2025Article
- N-Glycosylation of Antibodies: Biological Effects During Infections and Therapeutic Applications.Antibodies (Basel, Switzerland) · 2025Review
- A Surface Plasmon Resonance-Based Integrated Assay for Quantification and Glycosylation Characterization of Monoclonal Antibodies in Crude Heterogeneous Samples.Biotechnology and bioengineering · 2025Article
- IgG-Fc Glycosylation and a Novel Flowcytometric Assay to Predict Hemolytic Disease of the Fetus and Newborn.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2025Article
- Neutralizing Antibodies vs. Viruses: Interacting Mechanisms and Escape Tactics.Microorganisms · 2025Review
- Modeling glycans with AlphaFold 3: capabilities, caveats, and limitations.Glycobiology · 2025Article
- Impact of Monoclonal Antibody Aggregates on Effector Function Characterization.Antibodies (Basel, Switzerland) · 2025Article
- Altered Spike Immunoglobulin G Fc N-Linked Glycans Are Associated With Hyperinflammatory State in Adult Coronavirus Disease 2019 and Multisystem Inflammatory Syndrome in Children.Open forum infectious diseases · 2024Article
- Article
- Review
- One N-glycan regulates natural killer cell antibody-dependent cell-mediated cytotoxicity and modulates Fc γ receptor IIIa / CD16a structure.bioRxiv : the preprint server for biology · 2024Article
- Altered spike IgG Fc N-linked glycans are associated with hyperinflammatory state in adult COVID and Multisystem Inflammatory Syndrome in Children.medRxiv : the preprint server for health sciences · 2024Article
- Review
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Therapeutic monoclonal antibodies (mAbs) are largely based on the immunoglobulin G1 (IgG1) scaffold, and many elicit a cytotoxic cell-mediated response by binding Fc γ receptors. Core fucosylation, a prevalent modification to the asparagine (N)-linked carbohydrate on the IgG1 crystallizable fragment (Fc), decreases the Fc γ receptor IIIa (CD16a) binding affinity and mAb efficacy. We determined IgG1 Fc fucosylation reduced the CD16a affinity by 1.7 ± 0.1 kcal/mol when compared to that of afucosylated IgG1 Fc; however, CD16a N-glycan truncation decreased this penalty by 1.2 ± 0.1 kcal/mol or 70%. Fc fucosylation restricted the manifold of conformations sampled by displacing the CD16a Asn162-glycan that impinges upon the linkage between the α-mannose(1-6)β-mannose residues and promoted contacts with the IgG Tyr296 residue. Fucosylation also impacted the IgG1 Fc structure as indicated by changes in resonance frequencies and nuclear spin relaxation observed by solution nuclear magnetic resonance spectroscopy. The effects of fucosylation on IgG1 Fc may account for the remaining 0.5 ± 0.1 kcal/mol penalty of fucosylated IgG1 Fc binding CD16a when compared to that of afucosylated IgG1 Fc. Our results indicated the CD16a Asn162-glycan modulates the antibody affinity indirectly by reducing the volume sampled, as opposed to a direct mechanism with intermolecular glycan-glycan contacts previously proposed to stabilize this system. Thus, antibody engineering to enhance intermolecular glycan-glycan contacts will likely provide limited improvement, and future designs should maximize the affinity by maintaining the CD16a Asn162-glycan conformational heterogeneity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.