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Glycomics Profiling of Chinese Hamster Ovary Cell Glycosylation Mutants Reveals N-Glycans of a Novel Size and Complexity
Open accessAbstract
Identifying biological roles for mammalian glycans and the pathways by which they are synthesized has been greatly facilitated by investigations of glycosylation mutants of cultured cell lines and model organisms. Chinese hamster ovary (CHO) glycosylation mutants isolated on the basis of their lectin resistance have been particularly useful for glycosylation engineering of recombinant glycoproteins. To further enhance the application of these mutants, and to obtain insights into the effects of altering one specific glycosyltransferase or glycosylation activity on the overall expression of cellular glycans, an analysis of the N-glycans and major O-glycans of a panel of CHO mutants was performed using glycomic analyses anchored by matrix-assisted laser desorption ionization-time of flight/time of flight mass spectrometry. We report here the complement of the major N-glycans and O-glycans present in nine distinct CHO glycosylation mutants. Parent CHO cells grown in monolayer versus suspension culture had similar profiles of N- and O-GalNAc glycans, although the profiles of glycosylation mutants Lec1, Lec2, Lec3.2.8.1, Lec4, LEC10, LEC11, LEC12, Lec13, and LEC30 were consistent with available genetic and biochemical data. However, the complexity of the range of N-glycans observed was unexpected. Several of the complex N-glycan profiles contained structures of m/z approximately 13,000 representing complex N-glycans with a total of 26 N-acetyllactosamine (Gal beta1-4GlcNAc)(n) units. Importantly, the LEC11, LEC12, and LEC30 CHO mutants exhibited unique complements of fucosylated complex N-glycans terminating in Lewis(x) and sialyl-Lewis(x) determinants. This analysis reveals the larger-than-expected complexity of N-glycans in CHO cell mutants that may be used in a broad variety of functional glycomics studies and for making recombinant glycoproteins.
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“Advances in various omics technologies have significantly improved our understanding of CHO cells at different levels and enabled the rational targeting of glycosylation effectors for improved biopharmaceutical production [27,71,72,150–152].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [27]
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“when NeuAc is α2,3-linked (main sialylated species in CHO-derived glycoproteins) the conformational stability of the CH2 domain of IgG can be reduced, most likely a result of a steric effect between the protein backbone and the α2,3-sialylated 6-arm [27,28].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [27]
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“CHO cells do not express alpha-1,3-galactosyltransferases, which produce the immunogenic alpha-galactosyl epitope (although they have the gene), and the expression of CMP-N-acetylneuraminic acid hydroxylase, which produces CMP-NeuGc, is virtually absent [27,71,72].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [27]
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Hall, M. K., Hatchett, C. J., Khan, H. A., Lewis, H., & Schwalbe, R. A. (2025) · International Journal of Translational Medicine · doi:10.3390/ijtm5030036
Konada, R. S. R., Nischan, N., Silva, A., & Kohler, J. J. (2026) · Glycobiology · doi:10.1093/glycob/cwag011
Ingénierie métabolique de la voie de N-Glycosylation chez la diatomée Phaeodactylum tricornutum
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Computationally inspired glycoengineering to maximise mAb β4-galactosylation
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Glycome remodeling programs pathogenic γδ T17 cell responses in autoimmunity
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Metadata
- Authors
- North, S. J., Huang, H.-H., Sundaram, S., Jang-Lee, J., Etienne, A. T., Trollope, A., Chalabi, S., Dell, A., Stanley, P., & Haslam, S. M.
- Affiliations
- Imperial College London (GB)
- Albert Einstein College of Medicine (US)
- Corresponding author
- Stanley, Pamela
- Haslam, Stuart M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 285
- Issue
- 8
- Pages
- 5759-5775
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2820803
- OpenAlex
- W2033604747
- Cited by
- 207
- References
- 44
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 10 · 2021: 12 · 2020: 11 · 2019: 15 · 2018: 17 · 2017: 16 · 2016: 8 · 2015: 11 · 2014: 21 · 2013: 17 · 2012: 13
- FWCI
- 5.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- National Institutes of Health
- Directorate for Biological Sciences
- U.S. Public Health Service (NCI RO1-36434)
- Biotechnology and Biological Sciences Research Council (BB/F008309/1, B19088)
- National Cancer Institute
- National Institute of General Medical Sciences (GM 62116, U54GM062116)
- 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
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- glycosylation mutants, CHO cells, N-glycans, O-glycans, glycomics, lectin resistance, glycosyltransferases, N-acetyllactosamine, fucosylated N-glycans, CD15, sialyl Lewis X
- MeSH terms
- Animals, Carbohydrate Sequence, Cricetulus, Glycosylation, Cricetinae, Mutation, Polysaccharides, CHO Cells
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