ArticlemAbs2015
A novel in vitro assay to predict neonatal Fc receptor-mediated human IgG half-life.
Article in mAbs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Effect of oregano essential oil on intestinal immunoglobulin G in Holstein dairy bulls.Frontiers in veterinary science · 2024Article
- Population pharmacokinetics of belantamab mafodotin, a BCMA-targeting agent in patients with relapsed/refractory multiple myeloma.CPT: pharmacometrics & systems pharmacology · 2021Article
- Blocking Borrelia burgdorferi transmission from infected ticks to nonhuman primates with a human monoclonal antibody.The Journal of clinical investigation · 2021Article
- Improving priors for human monoclonal antibody linear pharmacokinetic parameters by using half-lives from non-human primates.Journal of pharmacokinetics and pharmacodynamics · 2021Article
- In Translation: FcRn across the Therapeutic Spectrum.International journal of molecular sciences · 2021Review
- Recent Achievements and Challenges in Prolonging the Serum Half-Lives of Therapeutic IgG Antibodies Through Fc Engineering.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2021Review
- Estrogen-Driven Changes in Immunoglobulin G Fc Glycosylation.Experientia supplementum (2012) · 2021Review
- Selecting and engineering monoclonal antibodies with drug-like specificity.Current opinion in biotechnology · 2019Review
- AnmAbs · 2019Article
- Article
- Effects of N-Glycosylation on the Structure, Function, and Stability of a Plant-Made Fc-Fusion Anthrax Decoy Protein.Frontiers in plant science · 2019Article
- Toward a Combinatorial Approach for the Prediction of IgG Half-Life and Clearance.Drug metabolism and disposition: the biological fate of chemicals · 2018Article
- Enhanced anti-metastatic bioactivity of an IGF-TRAP re-engineered to improve physicochemical properties.Scientific reports · 2018Article
- Next generation antibody drugs: pursuit of the 'high-hanging fruit'.Nature reviews. Drug discovery · 2018Review
- Antibody-mediated oral delivery of therapeutic DNA for type 2 diabetes mellitus.Biomaterials research · 2018Article
- Review
- Article
- A Two-pronged Binding Mechanism of IgG to the Neonatal Fc Receptor Controls Complex Stability and IgG Serum Half-life.Molecular & cellular proteomics : MCP · 2017Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin G (IgG) has an unusually long serum half-life in comparison to proteins of a similar size. It is well-known that this phenomenon is due to IgG's ability to bind the neonatal Fc receptor (FcRn) in a pH-dependent manner. FcRn binding properties can vary among IgGs, resulting in altered in vivo half-lives, and therefore it would be beneficial to accurately predict the FcRn binding properties of therapeutic IgG monoclonal antibodies (mAbs). Here we describe the development of an in vitro model capable of predicting the in vivo half-life of human IgG. Using a high-throughput biolayer interferometry (BLI) platform, the human FcRn association rate at acidic pH and subsequent dissociation rate at physiological pH was determined for 5 human IgG1 mAbs. Comparing the combined FcRn association and dissociation rates to the Phase 1 clinical study half-lives of the mAbs resulted in a strong correlation. The correlation was also verified in vivo using mice transgenic for human FcRn. The model was used to characterize various factors that may influence FcRn-mAb binding, including mAb variable region sequence differences and constant region glycosylation patterns. Results indicated that the complementarity-determining regions of the heavy chain significantly influence the mAb's FcRn binding properties, while the absence of glycosylation does not alter mAb-FcRn binding. Development of this high-throughput FcRn binding model could potentially predict the half-life of therapeutic IgGs and aid in selection of lead candidates while also serving as a screening tool for the development of mAbs with desired pharmacokinetic properties.
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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.