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Cited by 48Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsMonoclonal and Polyclonal Antibodies Research

Enhancement of sialylation on humanized IgG-like bispecific antibody by overexpression of α2,6-sialyltransferase derived from Chinese hamster ovary cells

Onitsuka, Masayoshi, Kim, Wook-Dong, Ozaki, Hiroyuki, Kawaguchi, Akira, Honda, Kohsuke, Kajiura, Hiroyuki, Fujiyama, Kazuhito, Asano, Ryutaro +3 more·2012·Applied Microbiology and Biotechnology
DOI 10.1007/s00253-011-3814-1
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Abstract

Improvement of glycosylation is one of the most important topics in the industrial production of therapeutic antibodies. We have focused on terminal sialylation with alpha-2,6 linkage, which is crucial for anti-inflammatory activity. In the present study, we have successfully cloned cDNA of beta-galactosyl alpha-2,6 sialyltransferase (ST6Gal I) derived from Chinese hamster ovary (CHO) cells regardless of reports that stated this was not endogenously expressed in CHO cells. After expressing cloned ST6Gal I in Escherichia coli, the transferase activity was confirmed by HPLC and lectin binding assay. Then, we applied ST6Gal I to alpha-2,6 sialylation of the recombinant antibody; the ST6Gal I expression vector was transfected into the CHO cell line producing a bispecific antibody. The N-glycosylation pattern of the antibody was estimated by HPLC and sialidase digestion. About 70% of the total N-linked oligosaccharide was alpha-2,6 sialylated in the transfected cell line whereas no sialylation was observed in the non-transfected cell line. The improvement of sialylation would be of practical importance for the industrial production of therapeutic antibodies.

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Crossref · 10.1007/s00253-011-3814-1

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  • Transient transfection of the Chinese hamster ST6Gal1 gene in CHO cells expressing a bispecific antibody also considerably increased the level of α2,6 sialylation.

    “Finally, transient transfection of the Chinese hamster ST6Gal1 gene in CHO cells expressing a bispecific antibody, also considerably increased the level of α2,6 sialylation (Onitsuka et al., 2012).”

    From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Onitsuka et al., 2012

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Authors
Onitsuka, M., Kim, W.-D., Ozaki, H., Kawaguchi, A., Honda, K., Kajiura, H., Fujiyama, K., Asano, R., Kumagai, I., Ohtake, H., & Omasa, T.
Affiliations
  • Tokushima University (JP)
  • The University of Osaka (JP)
  • International Center for Biotechnology, The University of Osaka (JP)
  • Tohoku University (JP)
ORCID
Venue
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2011-12-29
Volume
94
Issue
1
Pages
69-80
ISSN
  • 0175-7598 (ISSN-L)
  • 1432-0614
DOI
10.1007/s00253-011-3814-1
OpenAlex
W1990345672
Cited by
48
References
3
Citations by year
2026: 2 · 2023: 3 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 7 · 2018: 3 · 2017: 1 · 2016: 5 · 2015: 6 · 2014: 3 · 2013: 9 · 2012: 2
FWCI
1.82
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Applied Microbiology and Biotechnology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Institut national de la recherche scientifique
  • National Institute of Biomedical Innovation
  • Japan Society for the Promotion of Science (23360371, 23686118)
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
  • Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
Keywords
alpha-2,6-sialyltransferase, ST6Gal I, bispecific antibodies, antibody glycosylation, N-glycans, CHO cell transfection, recombinant antibody production, anti-inflammatory activity, Escherichia coli expression
MeSH terms
beta-D-Galactoside alpha 2-6-Sialyltransferase, Animals, Escherichia coli, Female, Cricetinae, Humans, Immunoglobulin G, Ovary, Recombinant Proteins, Sialyltransferases, Up-Regulation, Gene Expression, CHO Cells, Antibodies, Bispecific, Antibodies, Monoclonal, Humanized

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