ArticlemAbs2015
The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity.
Article in mAbs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
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Who cites it
123 citing papers in PubMed, 186 citations in OpenAlex.
- Neonatal Fc receptor antagonist efgartigimod safely and sustainably reduces IgGs in humans.The Journal of clinical investigation · 2018Trial
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- Physiologically based pharmacokinetic modeling of mRNA therapeutics: A multiscale framework for LNP and antibody trafficking in mice.Molecular therapy. Nucleic acids · 2026Article
- Folding-mediated secretion of pure bispecific antibodies.Nature biotechnology · 2026Article
- Nanobody-based targeted cancer therapy and immunotherapy: fear not the future.Acta pharmacologica Sinica · 2026Review
- Physiologically Based Pharmacokinetic Model to Predict Drug-Drug Interactions With the Antibody-Drug Conjugate Trastuzumab Deruxtecan.CPT: pharmacometrics & systems pharmacology · 2026Article
- Integrating In-vitro Permeability Assays within PBPK Modeling to Predict CNS Distribution of Standard and Engineered Antibodies.The AAPS journal · 2026Article
- Integrative structural insights into the IgG-FcRn interactions revealed by engineered FcRn-immobilized affinity chromatography.Communications biology · 2026Article
- Characterizing pH-Dependent Interactions Between Immunoglobulin and the Neonatal Fc Receptor Using Surface Plasmon Resonance.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Blocking the neonatal Fc receptor as a novel approach to prevent cardiac neonatal lupus: a proof-of-concept study.Annals of the rheumatic diseases · 2026Article
- Human and porcine IgG subclasses differentially engage porcine Fc receptors.Discovery immunology · 2026Article
- Review
- Article
- Review
- Structure of the human astrovirus capsid spike in complex with the neonatal Fc receptor.Nature communications · 2025Article
- Regulation of immune responses to therapeutic factor VIII by transplacental delivery of Fc-fused immunodominant factor VIII domains or peptides.Haematologica · 2025Article
- GX-I7, a long-acting IL-7, safely and effectively increased peripheral CD8British journal of cancer · 2025Article
- Identification of a direct interaction between the Fab domains of IgG antibodies and human FcRn upon IgG-FcRn complex formation.Communications biology · 2025Article
- Targeting the Neonatal Fc Receptor in Autoimmune Diseases: Pipeline and Progress.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025Review
63 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neonatal Fc receptor (FcRn) is expressed by cells of epithelial, endothelial and myeloid lineages and performs multiple roles in adaptive immunity. Characterizing the FcRn/IgG interaction is fundamental to designing therapeutic antibodies because IgGs with moderately increased binding affinities for FcRn exhibit superior serum half-lives and efficacy. It has been hypothesized that 2 FcRn molecules bind an IgG homodimer with disparate affinities, yet their affinity constants are inconsistent across the literature. Using surface plasmon resonance biosensor assays that eliminated confounding experimental artifacts, we present data supporting an alternate hypothesis: 2 FcRn molecules saturate an IgG homodimer with identical affinities at independent sites, consistent with the symmetrical arrangement of the FcRn/Fc complex observed in the crystal structure published by Burmeister et al. in 1994. We find that human FcRn binds human IgG1 with an equilibrium dissociation constant (KD) of 760 ± 60 nM (N = 14) at 25°C and pH 5.8, and shows less than 25% variation across the other human subtypes. Human IgG1 binds cynomolgus monkey FcRn with a 2-fold higher affinity than human FcRn, and binds both mouse and rat FcRn with a 10-fold higher affinity than human FcRn. FcRn/IgG interactions from multiple species show less than a 2-fold weaker affinity at 37°C than at 25°C and appear independent of an IgG's variable region. Our in vivo data in mouse and rat models demonstrate that both affinity and avidity influence an IgG's serum half-life, which should be considered when choosing animals, especially transgenic systems, as surrogates.
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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.