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GlycoDelete engineering of mammalian cells simplifies N-glycosylation of recombinant proteins
Open accessAbstract
Heterogeneity in the N-glycans on therapeutic proteins causes difficulties for protein purification and process reproducibility and can lead to variable therapeutic efficacy. This heterogeneity arises from the multistep process of mammalian complex-type N-glycan synthesis. Here we report a glycoengineering strategy--which we call GlycoDelete--that shortens the Golgi N-glycosylation pathway in mammalian cells. This shortening results in the expression of proteins with small, sialylated trisaccharide N-glycans and reduced complexity compared to native mammalian cell glycoproteins. GlycoDelete engineering does not interfere with the functioning of N-glycans in protein folding, and the physiology of cells modified by GlycoDelete is similar to that of wild-type cells. A therapeutic human IgG expressed in GlycoDelete cells had properties, such as reduced initial clearance, that might be beneficial when the therapeutic goal is antigen neutralization. This strategy for reducing N-glycan heterogeneity on mammalian proteins could lead to more consistent performance of therapeutic proteins and modulation of biopharmaceutical functions.
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“Using this expression system for transient anti-CD-20 production, recombinant proteins had very short sialylated N-glycans with high homogeneity on the Fc domain and reduced affinity to FcγRs compared to proteins expressed in wild-type 293S.”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Meuris et al., 2014
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“GlycoDelete is an elegant glycoengineering strategy worth mentioning, which reduces glycan heterogeneity by expressing a Golgi-targeted endo-β-N-acetylglucosaminidase in HEK 293SGnTI(−) cells to produce GlcNAc N-glycan ‘stumps’ modified by galactosyltransferases and sialyltransferases to yield small sialylated trisaccharides [108].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [108]
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“Furthermore, to improve N-glycan homogeneity on therapeutic proteins, a technique called “GlycoDelete” engineering was also recently developed in HEK293S cells (Meuris et al., 2014).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Meuris et al., 2014
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1 retracted
RETRACTED: Dominant suppression of inflammation by glycan-hydrolyzed IgG
Nandakumar, K. S., Collin, M., Happonen, K. E., Croxford, A. M., Lundström, S. L., Zubarev, R. A., Rowley, M. J., Blom, A. M., & Holmdahl, R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301480110 · Cited by 20
RetractedSkyline: an open source document editor for creating and analyzing targeted proteomics experiments
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FcRn: the neonatal Fc receptor comes of age
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An improved colorimetric assay for interleukin 2
Tada, H., Shiho, O., Kuroshima, K.-I., Koyama, M., & Tsukamoto, K. (1986) · Journal of Immunological Methods · doi:10.1016/0022-1759(86)90183-3 · Cited by 871
Thermofluor-based high-throughput stability optimization of proteins for structural studies
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Glycosylation as a strategy to improve antibody-based therapeutics
Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829
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Self-citationIntracellular Signaling by the Unfolded Protein Response
Bernales, S., Papa, F. R., & Walter, P. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.122303.120200 · Cited by 543
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Dekkers, G., Treffers, L. W., Plomp, R., Bentlage, A. E. H., de Boer, M., Koeleman, C. A. M., Lissenberg‐Thunnissen, S. N., Visser, R., Brouwer, M. C., Mok, J. Y., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00877 · Cited by 365
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296
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Metadata
- Authors
- Meuris, L., Santens, F., Elson, G., Festjens, N., Boone, M., Dos Santos, A., Devos, S., Rousseau, F., Plets, E., Houthuys, E., Malinge, P., Magistrelli, G., Cons, L., Chatel, L., Devreese, B., & Callewaert, N.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Light Chain Bioscience (Switzerland) (CH)
- Ghent University (BE)
- Corresponding author
- Callewaert, Nico
- ORCID
- Venue
- Nature Biotechnology
- Published
- 2014-04-20
- Volume
- 32
- Issue
- 5
- Pages
- 485-489
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- PMC
- PMC7039703
- OpenAlex
- W1965443132
- Cited by
- 141
- References
- 31
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 5 · 2023: 10 · 2022: 8 · 2021: 12 · 2020: 16 · 2019: 7 · 2018: 22 · 2017: 16 · 2016: 15 · 2015: 16 · 2014: 6
- FWCI
- 7.25
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Funders
- Fonds Wetenschappelijk Onderzoek (G.0.541.08.N.10)
- Universiteit Gent
- Vlaamse regering
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- N-glycosylation, glycoengineering, recombinant protein expression, protein clearance, glycoprotein folding, biopharmaceuticals
- MeSH terms
- Animals, Glycosylation, Humans, Polysaccharides, Recombinant Proteins, Protein Engineering, Mice
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