ArticlemAbs2019
Antibody Fc engineering for enhanced neonatal Fc receptor binding and prolonged circulation half-life.
Article in mAbs, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
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The trial behind it
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
68 citing papers in PubMed, 103 citations in OpenAlex.
- SHR-1918, A Monoclonal Antibody Against Angiopoietin-Like 3, in Healthy Subjects: A Randomized, Double-Blind, Placebo-Controlled Study.Clinical pharmacokinetics · 2025Trial
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- A Functional Investigation of Antibody Fc-FcRn Variant Binding Guided by In Silico Free Energy Perturbation Methods.Journal of molecular biology · 2026Article
- Systemic Inflammation as a Modulator of FcRn-dependent IgG Pharmacokinetics: Implications for Broadly Neutralising Antibody Efficacy in HIV Prevention.Current HIV/AIDS reports · 2026Review
- Fusion with immunoglobulin Fc fragment enhances the immunogenicity of the African swine fever virus p30/p54 fusion protein.Applied microbiology and biotechnology · 2026Article
- B Cells and B Cell Depletion in Autoimmunity and Atherosclerosis.Life (Basel, Switzerland) · 2026Review
- Research progress and development strategies of antibody-oligonucleotide conjugates.Gene therapy · 2026Review
- A functional investigation of antibody Fc-FcRn variant binding guided bybioRxiv : the preprint server for biology · 2026Article
- Fc-Engineering Improves PET Imaging of Anti-Mesothelin VH-Fc across Multiple Tumor Mouse Models and Reveals Sex-Specific Renal Clearance.Bioconjugate chemistry · 2026Article
- Systematic Evaluation of Vector Sequence Elements in Isogenic CHO Cells for Improved Antibody Production.ACS synthetic biology · 2026Article
- Novel biopharmaceutical strategies: Fc-fusion protein technology.Frontiers in pharmacology · 2026Review
- Bispecific and multispecific T-cell engagers: advancing the future of immunotherapy.Antibody therapeutics · 2026Review
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- Review
- Pharmacological considerations for next-generation protein therapeutics in cardiovascular disease.The Journal of pharmacology and experimental therapeutics · 2025Review
- Cure of experimentalmBio · 2025Article
- Afucosylated broadly neutralizing antibodies targeting the HIV envelope elicit enhanced NK-cell-mediated cytotoxicity against HIV-infected CD4+ T-cell and macrophage targets.Journal of leukocyte biology · 2025Article
- Engineering FcRn binding kinetics dramatically extends antibody serum half-life and enhances therapeutic potential.Journal of biological engineering · 2025Article
- Beneath the surface in autoimmune hemolytic anemia: pathogenetic networks, therapeutic advancements and open questions.Frontiers in immunology · 2025Review
- Discovery and investigation of the truncation of the (GGGGS)n linker and its effect on the productivity of bispecific antibodies expressed in mammalian cells.Bioprocess and biosystems engineering · 2025Article
8 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 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neonatal Fc receptor (FcRn) promotes antibody recycling through rescue from normal lysosomal degradation. The binding interaction is pH-dependent with high affinity at low pH, but not under physiological pH conditions. Here, we combined rational design and saturation mutagenesis to generate novel antibody variants with prolonged half-life and acceptable development profiles. First, a panel of saturation point mutations was created at 11 key FcRn-interacting sites on the Fc region of an antibody. Multiple variants with slower FcRn dissociation kinetics than the wildtype (WT) antibody at pH 6.0 were successfully identified. The mutations were further combined and characterized for pH-dependent FcRn binding properties, thermal stability and the FcγRIIIa and rheumatoid factor binding. The most promising variants, YD (M252Y/T256D), DQ (T256D/T307Q) and DW (T256D/T307W), exhibited significantly improved binding to FcRn at pH 6.0 and retained similar binding properties as WT at pH 7.4. The pharmacokinetics in human FcRn transgenic mice and cynomolgus monkeys demonstrated that these properties translated to significantly prolonged plasma elimination half-life compared to the WT control. The novel variants exhibited thermal stability and binding to FcγRIIIa in the range comparable to clinically validated YTE and LS variants, and showed no enhanced binding to rheumatoid factor compared to the WT control. These engineered Fc mutants are promising new variants that are widely applicable to therapeutic antibodies, to extend their circulation half-life with obvious benefits of increased efficacy, and reduced dose and administration frequency.
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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.