Cited by 265Monoclonal and Polyclonal Antibodies ResearchProtein purification and stabilityBiosimilars and Bioanalytical Methods

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Reduced elimination of IgG antibodies by engineering the variable region

Igawa, T., Tsunoda, H., Tachibana, T., Maeda, A., Mimoto, F., Moriyama, C., Nanami, M., Sekimori, Y., Nabuchi, Y., Aso, Y., Hattori, K.·2010·Protein Engineering Design and Selection

DOI 10.1093/protein/gzq009

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Abstract

Fc engineering to increase the binding affinity of IgG antibodies to FcRn has been reported to reduce the elimination of IgG antibodies. Herein, we present a novel non-FcRn-dependent approach to reduce the elimination of IgG antibodies. Pharmacokinetic studies conducted in normal mice of various humanized IgG4 antibodies, which had identical constant regions but different variable region sequences, revealed that an antibody with a lower isoelectric point (pI) has a longer half-life. These antibodies exhibited comparable binding affinity to FcRn, and with the antibodies with lower pIs, a longer half-life was also observed in beta2-microglobulin knockout mice, suggesting that differences in the pharmacokinetics were due to a non-FcRn-dependent mechanism. On the basis of our findings, we attempted to engineer the pharmacokinetic properties of a humanized anti-IL6 receptor IgG1 antibody. Selected substitutions in the variable region, without substitution in the Fc region, lowered the pI but did not reduce the biological activity and showed a significant reduction in the clearance of the antibody in cynomolgus monkey. These results suggest that lowering the pI by engineering the variable region could reduce the elimination of IgG antibodies and could provide an alternative to Fc engineering of IgG antibodies.

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A JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
Lindemann, L., Jaeschke, G., Michalon, A., Vieira, E., Honer, M., Spooren, W., Porter, R., Hartung, T., Kolczewski, S., Büttelmann, B., et al. (1909) · JAMA · doi:10.1001/jama.1909.02550020033007 · Cited by 7,889
Antibody Pharmacokinetics and Pharmacodynamics
Lobo, E. D., Hansen, R. J., & Balthasar, J. P. (2004) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20178 · Cited by 909
Challenges in the development of high protein concentration formulations
Shire, S. J., Shahrokh, Z., & 刘, J. 军. L. (2004) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20079 · Cited by 886
Generation of tissue-specific and promiscuous HLA ligand databases using DNA microarrays and virtual HLA class II matrices
Sturniolo, T., Bono, E. B., Ding, J., Raddrizzani, L., Tuereci, O., Şahin, U., Braxenthaler, M., Gallazzi, F., Protti, M. P., Sinigaglia, F., et al. (1999) · Nature Biotechnology · doi:10.1038/9858 · Cited by 743
Challenges in the Development of High Protein Concentration Formulations
Shire, S. J., Shahrokh, Z., & Liu, J. (2009) · Springer eBooks · doi:10.1007/978-0-387-76643-0_9 · Cited by 657
Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn)
Dall’Acqua, W. F., Kiener, P. A., & Wu, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604292200 · Cited by 648
Stability engineering of antibody single-chain Fv fragments
Wörn, A., & Plückthun, A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4265 · Cited by 616
Therapeutic antibodies for human diseases at the dawn of the twenty-first century
Brekke, O. H., & Sandlie, I. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd984 · Cited by 572
Differences in promiscuity for antibody–FcRn interactions across species: implications for therapeutic antibodies
Ober, R. J., Radu, C. G., Ghetie, V. F., & Ward, E. S. (2001) · International Immunology · doi:10.1093/intimm/13.12.1551 · Cited by 502
Elimination mechanisms of therapeutic monoclonal antibodies
Tabrizi, M. A., Tseng, C.-M. L., & Roskos, L. K. (2006) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03638-x · Cited by 479

Show all 44 references

Research works printed but not linked: 4

Almagro, 2008, Frontiers in bioscience : a journal and virtual library, 13, 1619
Devenny, 1985, Microcirculation, endothelium, and lymphatics, 2, 15
Kobayashi, 1999, Cancer Research, 59, 422
Onda, 2001, Cancer Research, 61, 5070

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“Therefore, characterization of charge variants is a critical quality attribute necessary to guarantee product safety, efficacy, and stability and it is also a regulatory requirement [21, 35–37].”
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Dumet, C. (2020) · theses.fr (ABES) · doi:10.70675/5a9ec911z0a71z4e28zbe61za14331956923
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Jones, T. D. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5041-7_17
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“Some studies have shown a lack of interplay between the variant pI and pharmacokinetics [112,115,116]; however, several other studies have indicated a decrease in the therapeutic potency of acidic variants compared to the main and basic variants and an increase in the potency of basic variants…”
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Authors: Igawa, T., Tsunoda, H., Tachibana, T., Maeda, A., Mimoto, F., Moriyama, C., Nanami, M., Sekimori, Y., Nabuchi, Y., Aso, Y., & Hattori, K.
Affiliations: Chugai Pharmaceutical Co., Ltd. (Japan) (JP)
ORCID: Igawa, T.
Tsunoda, H.
Tachibana, T.
Maeda, A.
Mimoto, F.
Hattori, K.
Venue: Protein Engineering Design and Selection
Publisher: Oxford University Press (OUP)
Published: 2010-02-15
Volume: 23
Issue: 5
Pages: 385-392
ISSN: 0269-2139 (ISSN-L)
1741-0126
1741-0134
DOI: 10.1093/protein/gzq009
OpenAlex: W2104198642
Cited by: 265
References: 44
Citations by year: 2026: 12 · 2025: 8 · 2024: 15 · 2023: 21 · 2022: 20 · 2021: 22 · 2020: 14 · 2019: 19 · 2018: 25 · 2017: 22 · 2016: 12 · 2015: 22 · 2014: 12 · 2013: 12 · 2012: 17
FWCI: 10.67
Type: journal article
Language: en
Open access: closed
Locations: Protein Engineering Design and Selection (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
Keywords: antibody half-life, isoelectric point, humanized monoclonal antibody, IgG4 antibodies, pharmacokinetics, Macaca fascicularis, antibody clearance
MeSH terms: Animals, Antibodies, Monoclonal, Cricetulus, Genetic Engineering, Half-Life, Cricetinae, Humans, Immunoglobulin G, Immunoglobulin Variable Region, Isoelectric Point, Receptors, Fc, Protein Engineering, Histocompatibility Antigens Class I, CHO Cells, Mice

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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Reduced elimination of IgG antibodies by engineering the variable region

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