ArticleCurrent research in immunology2020
Impact of IgG1 N-glycosylation on their interaction with Fc gamma receptors.
Article in Current research in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Realizing the potential of agonistic antibody immunotherapy.Nature reviews. Drug discovery · 2026Review
- Glycoengineering of plant-produced Pembrolizumab enhances FcRn binding and extends serum half-life in mice.Biotechnology reports (Amsterdam, Netherlands) · 2025Article
- CRISPR/Cas9-Mediated Knockouts of the ALG3 and GNTI in N. benthamiana and Their Application to Pharmaceutical Production.Plant biotechnology journal · 2025Article
- A Surface Plasmon Resonance-Based Integrated Assay for Quantification and Glycosylation Characterization of Monoclonal Antibodies in Crude Heterogeneous Samples.Biotechnology and bioengineering · 2025Article
- Enzymatic Desialylation Enables Reliable Charge Variant Characterization of Highly Glycosylated and Sialylated Fc Fusion Proteins.ACS pharmacology & translational science · 2025Article
- Glycoprotein Preparation by Heterologous Expression.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Site-Specific Antibody Conjugation Using Modified BisectedBioconjugate chemistry · 2023Article
- Serum concentration of antigen-specific IgG can substantially bias interpretation of antibody-dependent phagocytosis assay readout.iScience · 2023Article
- Grafting Strategies of Oxidation-Prone Coiled-Coil Peptides for Protein Capture in Bioassays: Impact of Orientation and the Oxidation State.ACS omega · 2023Article
- Generation of a symmetrical trispecific NK cell engager based on a two-in-one antibody.Frontiers in immunology · 2023Article
- Function-structure approach reveals novel insights on the interplay of Immunoglobulin G 1 proteoforms and Fc gamma receptor IIa allotypes.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
- SARS-CoV-2 infection of phagocytic immune cells and COVID-19 pathology: Antibody-dependent as well as independent cell entry.Frontiers in immunology · 2022Review
- Design of a Trispecific Checkpoint Inhibitor and Natural Killer Cell Engager Based on a 2 + 1 Common Light Chain Antibody Architecture.Frontiers in immunology · 2021Article
- Impact of Glycosylation and Species Origin on the Uptake and Permeation of IgGs through the Nasal Airway Mucosa.Pharmaceutics · 2020Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The effector functions of the IgGs are modulated by the N-glycosylation of their Fc region. Particularly, the absence of core fucosylation is known to increase the affinity of IgG1s for the Fcγ receptor IIIa expressed by immune cells, in turn translating in an improvement in the antibody-dependent cellular cytotoxicity. However, the impact of galactosylation and sialylation is still debated in the literature. In this study, we have investigated the influence of high and low levels of core fucosylation, terminal galactosylation and terminal α2,6-sialylation of the Fc N-glycans of trastuzumab on its affinity for the FcγRIIIa. A large panel of antibody glycoforms (i.e., highly α2,6-sialylated or galactosylated IgG1s, with high or low levels of core fucosylation) were generated and characterized, while their interactions with the FcγRs were analysed by a robust surface plasmon resonance-based assay as well as in a cell-based reporter bioassay. Overall, IgG1 glycoforms with reduced fucosylation display a stronger affinity for the FcγRIIIa. In addition, fucosylation, and the presence of terminal galactose and sialic acids are shown to increase the affinity for the FcγRIIIa as compared to the agalactosylated forms. These observations perfectly translate in the response observed in our reporter bioassay.
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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.