Production of α2,6-sialylated IgG1 in CHO cells
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The presence of α2,6-sialic acids on the Fc N-glycan provides anti-inflammatory properties to the IgGs through a mechanism that remains unclear. Fc-sialylated IgGs are rare in humans as well as in industrial host cell lines such as Chinese hamster ovary (CHO) cells. Facilitated access to well-characterized α2,6-sialylated IgGs would help elucidate the mechanism of this intriguing IgG's effector function. This study presents a method for the efficient Fc glycan α2,6-sialylation of a wild-type and a F243A IgG1 mutant by transient co-expression with the human α2,6-sialyltransferase 1 (ST6) and β1,4-galactosyltransferase 1 (GT) in CHO cells. Overexpression of ST6 alone only had a moderate effect on the glycoprofiles, whereas GT alone greatly enhanced Fc-galactosylation, but not sialylation. Overexpression of both GT and ST6 was necessary to obtain a glycoprofile dominated by α2,6-sialylated glycans in both antibodies. The wild-type was composed of the G2FS(6)1 glycan (38%) with remaining unsialylated glycans, while the mutant glycoprofile was essentially composed of G2FS(6)1 (25%), G2FS(3,6)2 (16%) and G2FS(6,6)2 (37%). The α2,6-linked sialic acids represented over 85% of all sialic acids in both antibodies. We discuss how the limited sialylation level in the wild-type IgG1 expressed alone or with GT results from the glycan interaction with Fc's amino acid residues or from intrinsic galactosyl- and sialyl-transferases substrate specificities.
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Co-expression of ST6Gal1 and β4GalT1 in CHO cells also significantly enhanced the sialylation level of the mutated version of trastuzumab.
“Co-expression of ST6Gal1 and β4GalT1 in CHO cells also significantly enhanced the sialylation level of the mutated version of trastuzumab (Raymond et al., 2015).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Raymond et al., 2015
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- Authors
- Raymond, C., Robotham, A., Spearman, M., Butler, M., Kelly, J., & Durocher, Y.
- Affiliations
- National Research Council Canada (CA)
- University of Manitoba (CA)
- Corresponding author
- Durocher, Yves
- Venue
- mAbs
- Publisher
- Informa UK Limited
- Published
- 2015-04-15
- Volume
- 7
- Issue
- 3
- Pages
- 571-583
- ISSN
- 1942-0862 (ISSN-L)
- 1942-0870
- PMC
- PMC4622614
- OpenAlex
- W1592578892
- Cited by
- 106
- References
- 65
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 10 · 2023: 10 · 2022: 6 · 2021: 10 · 2020: 9 · 2019: 11 · 2018: 12 · 2017: 11 · 2016: 9 · 2015: 7
- FWCI
- 5.65
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- mAbs (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- NPARC (submittedVersion)
- Funders
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Keywords
- α2,6-sialylation, IgG1, Fc glycan, sialic acid, beta-1,4-galactosyltransferase, CHO cells, antibody glycosylation
- MeSH terms
- beta-D-Galactoside alpha 2-6-Sialyltransferase, Animals, Antibodies, Monoclonal, Cricetulus, Cricetinae, Humans, Immunoglobulin G, N-Acetyllactosamine Synthase, Sialic Acids, Sialyltransferases, Antigens, CD, CHO Cells, Amino Acid Substitution, Mutation, Missense
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