ArticleScientific reports2019
The Fab portion of immunoglobulin G contributes to its binding to Fcγ receptor III.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 49 citations in OpenAlex.
- Effect of ADCC-enhancing mutations on N-glycan profiles of human IgG1 antibodies.The Biochemical journal · 2026Article
- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
- Review
- 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
- New insights into antibody structure with implications for specificity, variable region restriction and isotype choice.Nature reviews. Immunology · 2025Review
- FcγR binding differentially contributes to protection by two human monoclonal antibodies targetingScience translational medicine · 2025Article
- Review
- Antigen binding triggers long-range conformational changes in monoclonal antibodies.Frontiers in immunology · 2025Article
- Identification of potential C1-binding sites in the immunoglobulin CL domains.International immunology · 2024Article
- Factor VIII moiety of recombinant Factor VIII Fc fusion protein impacts Fc effector function and CD16Frontiers in immunology · 2024Article
- Identification of Mispairing Omic Signatures in Chinese Hamster Ovary (CHO) Cells Producing a Tri-Specific Antibody.Biomedicines · 2023Article
- Biophysical Characterization of the Contribution of the Fab Region to the IgG-FcγRIIIa Interaction.Biochemistry · 2023Article
- Negative interference with antibody-dependent cellular cytotoxicity mediated by rituximab from its interactions with human serum proteins.Frontiers in immunology · 2023Article
- Improving the efficacy of plant-made anti-HIV monoclonal antibodies for clinical use.Frontiers in plant science · 2023Article
- IL-1β-dependent extravasation of preexisting lung-restricted autoantibodies during lung transplantation activates complement and mediates primary graft dysfunction.The Journal of clinical investigation · 2022Article
- Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CInternational journal of molecular sciences · 2022Article
- From CD16a Biology to Antibody-Dependent Cell-Mediated Cytotoxicity Improvement.Frontiers in immunology · 2022Review
- Evaluation of strategies to modify Anti-SARS-CoV-2 monoclonal antibodies for optimal functionality as therapeutics.PloS one · 2022Article
- Role of Fc Core Fucosylation in the Effector Function of IgG1 Antibodies.Frontiers in immunology · 2022Review
- Macrophages Impair TLR9 Agonist Antitumor Activity through Interacting with the Anti-PD-1 Antibody Fc Domain.Cancers · 2021Article
Corrections and comments
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Authors and funding
17 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most cells active in the immune system express receptors for antibodies which mediate a variety of defensive mechanisms. These receptors interact with the Fc portion of the antibody and are therefore collectively called Fc receptors. Here, using high-speed atomic force microscopy, we observe interactions of human, humanized, and mouse/human-chimeric immunoglobulin G1 (IgG1) antibodies and their cognate Fc receptor, FcγRIIIa. Our results demonstrate that not only Fc but also Fab positively contributes to the interaction with the receptor. Furthermore, hydrogen/deuterium exchange mass spectrometric analysis reveals that the Fab portion of IgG1 is directly involved in its interaction with FcγRIIIa, in addition to the canonical Fc-mediated interaction. By targeting the previously unidentified receptor-interaction sites in IgG-Fab, our findings could inspire therapeutic antibody engineering.
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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.