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Production platforms for biotherapeutic glycoproteins. Occurrence impact, and challenges of non-human sialylation
Open accessAbstract
One of the fastest growing fields in the pharmaceutical industry is the market for therapeutic glycoproteins. Today, these molecules play a major role in the treatment of various diseases, and include several protein classes, i.e., clotting factors, hormones, cytokines, antisera, enzymes, enzyme inhibitors, Ig-Fc-Fusion proteins, and monoclonal antibodies. Optimal glycosylation is critical for therapeutic glycoproteins, as glycans can influence their yield, immunogenicity and efficacy, which impact the costs and success of such treatments. While several mammalian cell expression systems currently used can produce therapeutic glycoproteins that are mostly decorated with human-like glycans, they can differ from human glycans by presenting two structures at the terminal and therefore most exposed position. First, natural human N-glycans are lacking the terminal Gal 1-3Gal (alpha-Gal) modification; and second, they do not contain the non-human sialic acid N-glycolylneuraminic acid (Neu5Gc). All humans spontaneously express antibodies against both of these glycan structures, risking increased immunogenicity of biotherapeutics carrying such non-human glycan epitopes. However, in striking contrast to the alpha-Gal epitope, exogenous Neu5Gc can be metabolically incorporated into human cells and presented on expressed glycoproteins in several possible epitopes. Recent work has demonstrated that this non-human sialic acid is found in widely varying amounts on biotherapeutic glycoproteins approved for treatment of various medical conditions. Neu5Gc on glycans of these medical agents likely originates from the production process involving the non-human mammalian cell lines and/or the addition of animal-derived tissue culture supplements. Further studies are needed to fully understand the impact of Neu5Gc in biotherapeutic agents. Similar concerns apply to human cells prepared for allo- or auto-transplantation, that have been grown in animal-derived tissue culture supplements.
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“Indeed, plants produce core α1,3-fructose and β1,2-xylose, which are completely absent in human cells and could be immunogenic (Karg et al., 2009;Ghaderi et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Ghaderi et al., 2012
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Metadata
- Authors
- Ghaderi, D., Zhang, M., Hurtado-Ziola, N., & Varki, A.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Varki, Ajit
- Venue
- Biotechnology and Genetic Engineering Reviews
- Publisher
- Informa UK Limited
- Published
- 2012-01
- Volume
- 28
- Issue
- 1
- Pages
- 147-176
- ISSN
- 0264-8725 (ISSN-L)
- 2046-5556
- OpenAlex
- W1997984454
- Cited by
- 320
- References
- 128
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 15 · 2023: 13 · 2022: 22 · 2021: 29 · 2020: 29 · 2019: 30 · 2018: 25 · 2017: 30 · 2016: 24 · 2015: 36 · 2014: 23 · 2013: 21 · 2012: 3
- FWCI
- 10.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biotechnology and Genetic Engineering Reviews (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 › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- N-glycolylneuraminic acid, alpha-gal epitope, therapeutic glycoproteins, biologic therapy, N-glycosylation, immunogenicity, sialic acid, monoclonal antibodies
- MeSH terms
- Animals, Antibodies, Monoclonal, Epitopes, Biotechnology, Carbohydrate Sequence, Cattle, Cells, Cultured, Culture Media, Disaccharides, Glycoproteins, Glycosylation, Cricetinae, Humans, Insecta, Rabbits, Recombinant Proteins, Sialic Acids, Swine, Cell Culture Techniques, Mice
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