Cited by 764Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsMonoclonal and Polyclonal Antibodies Research

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Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity

Umaña, Pablo, Jean–Mairet, Joël, Moudry, Radmila, Amstutz, Hanspeter, Bailey, James E.·1999·Nature Biotechnology

DOI 10.1038/6179

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Abstract

The glycosylation pattern of chCE7, an antineuroblastoma chimeric IgG1, was engineered in Chinese hamster ovary cells with tetracycline-regulated expression of beta(1,4)-N-acetylglucosaminyltransferase III (GnTIII), a glycosyltransferase catalyzing formation of bisected oligosaccharides that have been implicated in antibody-dependent cellular cytotoxicity (ADCC). Measurement of the ADCC activity of chCE7 produced at different tetracycline levels showed an optimal range of GnTIII expression for maximal chCE7 in vitro ADCC activity, and this activity correlated with the level of constant region-associated, bisected complex oligosaccharides determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The new optimized variants of chCE7 exhibit substantial ADCC activity and, hence, may be useful for treatment of neuroblastoma. The strategy presented here should be applicable to optimize the ADCC activity of other therapeutic IgGs.

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Dürr, U., Haldemann, A.R., Leibundgut, K., Novak–Hofer, I., Amstutz, H., Wagner, H.P., et al. 1993.First clinical results with the chimeric antibody chCE7 in neuroblastoma. Targeting features and biodistribution data. Eur. J. Nucl. Med. 20: 858.

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Authors: Umaña, P., Jean–Mairet, J., Moudry, R., Amstutz, H., & Bailey, J. E.
Affiliations: ETH Zurich (CH)
Swiss Red Cross (CH)
Corresponding author: Bailey, James E.
ORCID: Umaña, Pablo
Bailey, James E.
Venue: Nature Biotechnology
Publisher: Springer Science and Business Media LLC
Published: 1999-02
Volume: 17
Issue: 2
Pages: 176-180
ISSN: 0733-222X (ISSN-L)
1087-0156
1546-1696
DOI: 10.1038/6179
OpenAlex: W1518819083
Semantic Scholar: 91b684d5d7b8cdc532055ffbfcb872089efff9a2
Cited by: 764
References: 26
Citations by year: 2026: 11 · 2025: 15 · 2024: 14 · 2023: 17 · 2022: 13 · 2021: 28 · 2020: 28 · 2019: 29 · 2018: 39 · 2017: 31 · 2016: 40 · 2015: 43 · 2014: 40 · 2013: 35 · 2012: 38
FWCI: 4.25
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Biotechnology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Keywords: antibody glycosylation, glycoforms, antibody-dependent cellular cytotoxicity, neuroblastoma, tetracycline-regulated expression, CHO cells, therapeutic antibodies, glycosylation engineering
MeSH terms: Animals, Antibody-Dependent Cell Cytotoxicity, Carbohydrate Sequence, Cricetinae, Humans, Immunoglobulin G, Molecular Sequence Data, Neuroblastoma, Tetracycline, Gene Expression Regulation, Enzymologic, CHO Cells, N-Acetylglucosaminyltransferases

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Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity

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