ArticleScientific reports2018
Inhibition of poly-LacNAc biosynthesis with release of CMP-Neu5Ac feedback inhibition increases the sialylation of recombinant EPO produced in CHO cells.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Cell Engineering for Increasing Production of Recombinant Proteins in Mammalian Cells.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Ultradeep N-glycoproteome atlas of mouse reveals spatiotemporal signatures of brain aging and neurodegenerative diseases.Nature communications · 2025Article
- Recombinant Human CD19 in CHO-K1 Cells: Glycosylation Patterns as a Quality Attribute of High Yield Processes.International journal of molecular sciences · 2023Article
- Glycoengineering Chinese hamster ovary cells: a short history.Biochemical Society transactions · 2021Review
- Big-Data Glycomics: Tools to Connect Glycan Biosynthesis to Extracellular Communication.Trends in biochemical sciences · 2021Review
- Transfection of glycoprotein encoding mRNA for swift evaluation of N-glycan engineering strategies.Biotechnology progress · 2020Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
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Abstract
Sialylation of recombinant therapeutic glycoproteins modulates their pharmacokinetic properties by affecting their in vivo half-life. N-glycan branching on glycoproteins increases the number of potential attachment sites for sialic acid. Here, we introduce a new approach for increasing the sialylation of recombinant human erythropoietin (rhEPO) produced in CHO cells by modulating poly-N-acetyllactosamine (poly-LacNAc) biosynthesis. We did not observe an increase in rhEPO sialylation, however, until the feedback inhibition by intracellular cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac), which is a limiting factor for sialylation, was released. Thus, we found that a combined approach inhibiting poly-LacNAc biosynthesis and releasing CMP-Neu5Ac feedback inhibition produces the most significant increase in rhEPO sialylation in metabolically engineered CHO cells. Furthermore, a detailed analysis of the resulting N-glycan structures using LC/MS revealed increased tri- and tetra- sialylated N-glycan structures accompanied by a reduction of di-sialylated N-glycan structures. These results validate our new approach for glycosylation engineering, and we expect this approach will be useful in future efforts to enhance the efficacy of other therapeutic glycoproteins.
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