ArticlemAbs
Regulation of antibody-mediated complement-dependent cytotoxicity by modulating the intrinsic affinity and binding valency of IgG for target antigen.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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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
36 citing papers in PubMed, 62 citations in OpenAlex.
- Pathogenic properties of myasthenia gravis AChR autoantibodies associate with clinical response to efgartigimod.Journal of neurology, neurosurgery, and psychiatry · 2026Trial
- CD80 (B7-1) as a potential therapeutic target in Epstein-Barr virus‑associated B cell diseases.Scientific reports · 2026Article
- Lack of association between rheumatoid factor levels and clinical response to certolizumab pegol in patients with rheumatoid arthritis: an observational study.Drugs in context · 2026Article
- Review
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- High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect againstEmerging microbes & infections · 2025Article
- TNF-α x FcαRI bi-specific antibody potentiates neutrophil-mediated anti-tumor effects.Scientific reports · 2025Article
- Engineering affinity-matured variants of an anti-polysialic acid monoclonal antibody with superior cytotoxicity-mediating potency.Cell chemical biology · 2025Article
- Affinity Affects the Functional Potency of Anti-GD2 Antibodies by Target-Mediated Drug Disposition.Cancers · 2025Article
- Harnessing endogenous anti-glycan antibodies using a novel, bifunctional immunotherapy to treat gram-negative bacterial infections.Journal of immunology (Baltimore, Md. : 1950) · 2025Article
- Fc gamma receptor polymorphisms in antibody therapy: implications for bioassay development to enhance product quality.Antibody therapeutics · 2025Review
- Comparative Preclinical Evaluation of Tuznue Versus Referent Herceptin: A Registered Trastuzumab Biosimilar.Drugs in R&D · 2025Article
- Review
- Antibody Drug Conjugates (ADCs): Shaping the Future of Precision Oncology.Anti-cancer agents in medicinal chemistry · 2025Review
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- A Short Update on the Use of Monoclonal Antibodies in COVID-19.The AAPS journal · 2024Article
- Development of a recombinant human IgG1 monoclonal antibody against the TRBV5-1 segment of the T cell receptor for the treatment of mature T cell neoplasms.Frontiers in immunology · 2024Article
- Cancer drugs with high repositioning potential for Alzheimer's disease.Expert opinion on emerging drugs · 2023Review
- Fc-Engineered Therapeutic Antibodies: Recent Advances and Future Directions.Pharmaceutics · 2023Review
- Unlocking the Power of Complement-Dependent Cytotoxicity: Engineering Strategies for the Development of Potent Therapeutic Antibodies for Cancer Treatments.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement-dependent cytotoxicity (CDC) is a potent effector mechanism, engaging both innate and adaptive immunity. Although strategies to improve the CDC activity of antibody therapeutics have primarily focused on enhancing the interaction between the antibody crystallizable fragment (Fc) and the first subcomponent of the C1 complement complex (C1q), the relative importance of intrinsic affinity and binding valency of an antibody to the target antigen is poorly understood. Here we show that antibody binding affinity to a cell surface target antigen evidently affects the extent and efficacy of antibody-mediated complement activation. We further report the fundamental role of antibody binding valency in the capacity to recruit C1q and regulate CDC. More specifically, an array of affinity-modulated variants and functionally monovalent bispecific derivatives of high-affinity anti-epidermal growth factor receptor (EGFR) and anti-human epidermal growth factor receptor 2 (HER2) therapeutic immunoglobulin Gs (IgGs), previously reported to be deficient in mediating complement activation, were tested for their ability to bind C1q by biolayer interferometry using antigen-loaded biosensors and to exert CDC against a panel of EGFR and HER2 tumor cells of various histological origins. Significantly, affinity-reduced variants or monovalent derivatives, but not their high-affinity bivalent IgG counterparts, induced near-complete cell cytotoxicity in tumor cell lines that had formerly been shown to be resistant to complement-mediated attack. Our findings suggest that monovalent target engagement may contribute to an optimal geometrical positioning of the antibody Fc to engage C1q and deploy the complement pathway.
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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.