ArticlemAbs
Dimers and multimers of monoclonal IgG1 exhibit higher in vitro binding affinities to Fcgamma receptors.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Impact of Monoclonal Antibody Aggregates on Effector Function Characterization.Antibodies (Basel, Switzerland) · 2025Article
- Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease.The protein journal · 2025Review
- Can antibody conjugated nanomicelles alter the prospect of antibody targeted therapy against schistosomiasis mansoni?PLoS neglected tropical diseases · 2023Article
- Nanoplasmonic Avidity-Based Detection and Quantification of IgG Aggregates.Analytical chemistry · 2022Article
- Catastrophic Embolism Following Cosmetic Injection of Autologous Fat: Are Silicone-Treated Syringes the Only Suspects on the Crime Scene?Frontiers in surgery · 2022Article
- Intersection of FcγRIIB, the microbiome, and checkpoint inhibitors in antitumor immunity.Cancer immunology, immunotherapy : CII · 2021Review
- On the Use of Surface Plasmon Resonance Biosensing to Understand IgG-FcγR Interactions.International journal of molecular sciences · 2021Review
- Immunogenicity Risk Assessment for an Engineered Human Cytokine Analogue Expressed in Different Cell Substrates.The AAPS journal · 2020Review
- Considerations for the Design of Antibody-Based Therapeutics.Journal of pharmaceutical sciences · 2020Review
- Evaluation ofFrontiers in immunology · 2019Article
- Low pH Exposure During Immunoglobulin G Purification Methods Results in Aggregates That Avidly Bind Fcγ Receptors: Implications for Measuring Fc Dependent Antibody Functions.Frontiers in immunology · 2019Article
- A novel probe to assess cytosolic entry of exogenous proteins.Nature communications · 2018Article
- Aggregates of IVIG or Avastin, but not HSA, modify the response to model innate immune response modulating impurities.Scientific reports · 2018Article
- Enrichment of high affinity subclasses and glycoforms from serum-derived IgG using FcγRs as affinity ligands.Biotechnology and bioengineering · 2018Article
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- Human Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97.Viruses · 2018Article
- Systems serology: profiling vaccine induced humoral immunity against HIV.Retrovirology · 2017Review
- Rapid screening of IgG quality attributes - effects on Fc receptor binding.FEBS open bio · 2017Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The in vitro binding of monomeric, dimeric and multimeric forms of monoclonal IgG1 molecules, designated mAb1 and mAb2, to the extracellular domains of Fcgamma receptors RI, RIIA and RIIIB were investigated using a surface plasmon resonance (SPR) based biosensor technique. Stable noncovalent and covalent dimers of mAb1 and mAb2, respectively, were isolated from CHO cell expressed materials. The dissociation constants of monomeric mAb1 and mAb2 were determined to be 1 nM for the FcgammaRI-binding and 6-12 microM for the FcgammaRIIA- and FcgammaRIIIB-binding. Dimeric mAb1 and mAb2 exhibited increased affinities, by 2-3 fold for FcgammaRI and 200-800 fold for FcgammaRIIA and FcgammaRIIIB. Further increases in binding were observed when the antibodies formed large immune complexes with multivalent antigens, but not in a linear relation with size. The binding properties of monomeric mAb2 were identical with and without a bound monovalent antigen, indicating that antigen-binding alone does not induce measurable change in binding of antibodies to Fcgamma receptors. Dimerization is sufficient to show enhancement in the receptor binding. Given the wide distribution of the low-affinity Fcgamma receptors on immune effector cells, the increased affinities to aggregated IgG may lead to some biological consequences, depending on the subsequent signal transduction events. The SPR-based in vitro binding assay is useful in evaluating Fcgamma receptor binding of various species in antibody-based biotherapeutics.
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