ArticleScientific reports2017
Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa.
Article in Scientific reports, 2017. 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, 80 citations in OpenAlex.
- Dynamic inter-glycan interactions regulate site-specific N-glycan maturation in human Fcγ receptor III.Glycobiology · 2026Article
- Molecular Basis of Core Fucosylation-Dependent Modulation of IgG1 Fc-CD16a Binding.bioRxiv : the preprint server for biology · 2026Article
- De novo determination of fucose linkages in N-glycans using logically derived sequence tandem mass spectrometry.Glycoconjugate journal · 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
- Article
- PlasmaNeurology(R) neuroimmunology & neuroinflammation · 2025Article
- Glycosylation in neuroinflammation: mechanisms, implications, and therapeutic strategies for neurodegenerative diseases.Translational neurodegeneration · 2025Review
- 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
- Review
- Article
- 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
- Collision-Induced Dissociation of Fucose and Identification of Anomericity.The journal of physical chemistry. A · 2024Article
- Antibodies as key mediators of protection againstFrontiers in immunology · 2024Review
- Mechanism of glycoform specificity and in vivo protection by an anti-afucosylated IgG nanobody.Nature communications · 2023Article
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Review
- Afucosylated IgG responses in humans - structural clues to the regulation of humoral immunity.Trends in immunology · 2022Review
- Experimental and computational characterization of dynamic biomolecular interaction systems involving glycolipid glycans.Glycoconjugate journal · 2022Review
Corrections and comments
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Authors and funding
9 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibody-dependent cellular cytotoxicity (ADCC) is promoted through interaction between the Fc region of immunoglobulin G1 (IgG1) and Fcγ receptor IIIa (FcγRIIIa), depending on N-glycosylation of these glycoproteins. In particular, core fucosylation of IgG1-Fc N-glycans negatively affects this interaction and thereby compromises ADCC activity. To address the mechanisms of this effect, we performed replica-exchange molecular dynamics simulations based on crystallographic analysis of a soluble form of FcγRIIIa (sFcγRIIIa) in complex with IgG1-Fc. Our simulation highlights increased conformational fluctuation of the N-glycan at Asn162 of sFcγRIIIa upon fucosylation of IgG1-Fc, consistent with crystallographic data giving no interpretable electron density for this N-glycan, except for the innermost part. The fucose residue disrupts optimum intermolecular carbohydrate-carbohydrate interactions, rendering this sFcγRIIIa glycan distal from the Fc glycan. Moreover, our simulation demonstrates that core fucosylation of IgG1-Fc affects conformational dynamics and rearrangements of surrounding amino acid residues, typified by Tyr296 of IgG1-Fc, which was more extensively involved in the interaction with sFcγRIIIa without Fc core fucosylation. Our findings offer a structural foundation for designing and developing therapeutic antibodies with improved ADCC activity.
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