ArticleThe Journal of biological chemistry2012
Anti-carcinoembryonic antigen single-chain variable fragment antibody variants bind mouse and human neonatal Fc receptor with different affinities that reveal distinct cross-species differences in serum half-life.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Development of a Novel Engineered Antibody Format for PSMA-Targeted Radionuclide Therapy.Molecular pharmaceutics · 2025Article
- Integrating Biochemical and Computational Approaches Reveal Structural Insights in Trastuzumab scFv-Fc Antibody Engineering.Biomolecules · 2025Article
- The FcRn from gene to protein and function: comparison between species.Frontiers in immunology · 2025Review
- A fusion protein of vimentin with Fc fragment inhibits Japanese encephalitis virus replication.Frontiers in veterinary science · 2024Article
- Fc Engineering Strategies to Advance IgA Antibodies as Therapeutic Agents.Antibodies (Basel, Switzerland) · 2020Review
- Targeting B-cell malignancies with the beta-emitting anti-CD37 radioimmunoconjugateEuropean journal of nuclear medicine and molecular imaging · 2019Article
- Expression of Functional Anti-p24 scFv 183-H12-5C in HEK293T and Jurkat T Cells.Advanced pharmaceutical bulletin · 2017Article
- Expression System Based on an MTIIa Promoter to Produce hPSA in Mammalian Cell Cultures.Frontiers in microbiology · 2016Article
- Fc Engineering of Human IgG1 for Altered Binding to the Neonatal Fc Receptor Affects Fc Effector Functions.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
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- Humanized FcRn mouse models for evaluating pharmacokinetics of human IgG antibodies.Methods (San Diego, Calif.) · 2014Article
- Unraveling the Interaction between FcRn and Albumin: Opportunities for Design of Albumin-Based Therapeutics.Frontiers in immunology · 2014Review
- Binding structures and energies of the human neonatal Fc receptor with human Fc and its mutants by molecular modeling and dynamics simulations.Molecular bioSystems · 2013Article
- Chimeric anti-CD14 IGG2/4 Hybrid antibodies for therapeutic intervention in pig and human models of inflammation.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Selection of nanobodies that target human neonatal Fc receptor.Scientific reports · 2013Article
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Authors and funding
8 authors.
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Abstract
Serum half-life of IgG is controlled by the neonatal Fc receptor (FcRn) that interacts with the IgG Fc region and may be increased or decreased as a function of altered FcRn binding. Preclinical evaluations of modified IgGs are frequently carried out in mice, but such IgGs may bind differently to mouse and human FcRn (mFcRn and hFcRn). Here, we report a detailed characterization of a matched set of mouse-human chimeric T84.66 scFv-Fc variants with specificity for the tumor carcinoembryonic antigen and mutations in the FcRn-binding site. Binding to soluble mFcRn and hFcRn was measured using in vitro assays, and the results were compared with blood clearance in vivo in normal (mFcRn bearing) and hFcRn transgenic mice. All variants bound better to mFcRn than to hFcRn. The loss of affinity varied among the mutants, however, and also the hierarchy of binding differed depending on the receptor. The mutations had no major impact on binding to the classical Fcγ receptors. Importantly, the trend of blood clearance in both strains of mice correlated with the hierarchy of binding obtained using soluble FcRn. Consequently, in vitro interaction analysis of engineered IgGs regarding their cross-species FcRn binding ability provides information for prediction of in vivo pharmacokinetics.
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