ArticleJournal of immunology (Baltimore, Md. : 1950)2015
Fc Engineering of Human IgG1 for Altered Binding to the Neonatal Fc Receptor Affects Fc Effector Functions.
Article in Journal of immunology (Baltimore, Md. : 1950), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 87 citations in OpenAlex.
- Neonatal Fc receptor antagonist efgartigimod safely and sustainably reduces IgGs in humans.The Journal of clinical investigation · 2018Trial
- A third-generation, high-affinity biparatopic anti-tau antibody inhibits intracellular tau aggregation seeded by Alzheimer's brain extracts.Alzheimer's research & therapy · 2026Article
- Human herpesvirus evasion of humoral immunity and implications for vaccine development.Nature reviews. Microbiology · 2026Review
- The Effect of FcRn Binding on Ocular Disposition of Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2026Article
- The S190R mutation in RSV-A F protein impairs nirsevimab binding and neutralization capacity.Virus evolution · 2026Article
- Selective decoupling of IgG1 binding to viral Fc receptors restores antibody-mediated NK cell activation against HCMV.Cell reports · 2025Article
- Glycoengineering of plant-produced Pembrolizumab enhances FcRn binding and extends serum half-life in mice.Biotechnology reports (Amsterdam, Netherlands) · 2025Article
- Review
- Eliminating interactions with the viral Fc receptor improves antibody-mediated protection against neonatal HSV infection in mice.Science translational medicine · 2025Article
- Tailored collagen binding of albumin-fused hyperactive coagulation factor IX dictates in vivo distribution and functional properties.Nature communications · 2025Article
- Postmarketing adverse events of efgartigimod alfa: a real-world pharmacovigilance study based on the FAERS database.BMJ open · 2025Article
- Identification of a direct interaction between the Fab domains of IgG antibodies and human FcRn upon IgG-FcRn complex formation.Communications biology · 2025Article
- Enhanced plasma half-life and efficacy of engineered human albumin-fused GLP-1 despite enzymatic cleavage of its C-terminal end.Communications biology · 2025Article
- An intranasal subunit vaccine induces protective systemic and mucosal antibody immunity against respiratory viruses in mouse models.Nature communications · 2025Article
- Impact of Monoclonal Antibody Aggregates on Effector Function Characterization.Antibodies (Basel, Switzerland) · 2025Article
- Effect of FcRn Binding on Monoclonal Antibody Disposition in the Brain.The AAPS journal · 2025Article
- Fc-engineered antibodies promote neutrophil-dependent control of Mycobacterium tuberculosis.Nature microbiology · 2024Article
- Long-Acting Strategies for Antibody Drugs: Structural Modification, Controlling Release, and Changing the Administration Route.European journal of drug metabolism and pharmacokinetics · 2024Review
- Human IgG Fc-engineering for enhanced plasma half-life, mucosal distribution and killing of cancer cells and bacteria.Nature communications · 2024Article
- Decoupling FcRn and tumor contributions to elevated immune checkpoint inhibitor clearance in cancer cachexia.Pharmacological research · 2024Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Engineering of the constant Fc part of monoclonal human IgG1 (hIgG1) Abs is an approach to improve effector functions and clinical efficacy of next-generation IgG1-based therapeutics. A main focus in such development is tailoring of in vivo half-life and transport properties by engineering the pH-dependent interaction between IgG and the neonatal Fc receptor (FcRn), as FcRn is the main homeostatic regulator of hIgG1 half-life. However, whether such engineering affects binding to other Fc-binding molecules, such as the classical FcγRs and complement factor C1q, has not been studied in detail. These effector molecules bind to IgG1 in the lower hinge-CH2 region, structurally distant from the binding site for FcRn at the CH2-CH3 elbow region. However, alterations of the structural composition of the Fc may have long-distance effects. Indeed, in this study we show that Fc engineering of hIgG1 for altered binding to FcRn also influences binding to both the classical FcγRs and complement factor C1q, which ultimately results in alterations of cellular mechanisms such as Ab-dependent cell-mediated cytotoxicity, Ab-dependent cellular phagocytosis, and Ab-dependent complement-mediated cell lysis. Thus, engineering of the FcRn-IgG1 interaction may greatly influence effector functions, which has implications for the therapeutic efficacy and use of Fc-engineered hIgG1 variants.
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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.