ArticleBiotechnology progress
Chinese hamster ovary (CHO) host cell engineering to increase sialylation of recombinant therapeutic proteins by modulating sialyltransferase expression.
Article in Biotechnology progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 70 citations in OpenAlex.
- Pooled it
- The Role of Glycan Structures in Modulating GM-CSF Bioactivity: Insights from Glycoengineering.bioRxiv : the preprint server for biology · 2026Article
- Advancing recombinant protein production in CHO cells through metabolic engineering.Frontiers in bioengineering and biotechnology · 2026Review
- De novo sequencing of glycans by ion mobility-mass spectrometry using a self-expanding database.Nature communications · 2025Article
- N-Glycosylation of Antibodies: Biological Effects During Infections and Therapeutic Applications.Antibodies (Basel, Switzerland) · 2025Review
- Transcriptomic Insights Into Serum-Free Medium Adaptation and Temperature Reduction in Chinese Hamster Ovary Cell Cultures.Biotechnology journal · 2025Article
- Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- CRISPR Technologies in Chinese Hamster Ovary Cell Line Engineering.International journal of molecular sciences · 2023Review
- Beyond antibody fucosylation: α-(1,6)-fucosyltransferase (Fut8) as a potential new therapeutic target for cancer immunotherapy.Antibody therapeutics · 2023Review
- Engineering protein glycosylation in CHO cells to be highly similar to murine host cells.Frontiers in bioengineering and biotechnology · 2023Article
- Strategies and Considerations for Improving Recombinant Antibody Production and Quality in Chinese Hamster Ovary Cells.Frontiers in bioengineering and biotechnology · 2022Review
- Fc glycan sialylation of biotherapeutic monoclonal antibodies has limited impact on antibody-dependent cellular cytotoxicity.FEBS open bio · 2021Article
- Multiplexed engineering glycosyltransferase genes in CHO cells via targeted integration for producing antibodies with diverse complex-type N-glycans.Scientific reports · 2021Article
- Animal Cell Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Generation of FXBiotechnology progress · 2021Article
- Comparison of Three Glycoproteomic Methods for the Analysis of the Secretome of CHO Cells Treated with 1,3,4-Bioengineering (Basel, Switzerland) · 2020Article
- Enhancement of sialylation in rIgG in glyco-engineered Chinese hamster ovary cells.Cytotechnology · 2020Article
- Dissecting N-Glycosylation Dynamics in Chinese Hamster Ovary Cells Fed-batch Cultures using Time Course Omics Analyses.iScience · 2019Article
- N-glycome of the Lysosomal Glycocalyx is Altered in Niemann-Pick Type C Disease (NPC) Model Cells.Molecular & cellular proteomics : MCP · 2018Article
- Predictive glycoengineering of biosimilars using a Markov chain glycosylation model.Biotechnology journal · 2017Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
N-Glycans of human proteins possess both α2,6- and α2,3-linked terminal sialic acid (SA). Recombinant glycoproteins produced in Chinese hamster overy (CHO) only have α2,3-linkage due to the absence of α2,6-sialyltransferase (St6gal1) expression. The Chinese hamster ST6GAL1 was successfully overexpressed using a plasmid expression vector in three recombinant immunoglobulin G (IgG)-producing CHO cell lines. The stably transfected cell lines were enriched for ST6GAL1 overexpression using FITC-Sambucus nigra (SNA) lectin that preferentially binds α2,6-linked SA. The presence of α2,6-linked SA was confirmed using a novel LTQ Linear Ion Trap Mass Spectrometry (LTQ MS) method including MSn fragmentation in the enriched ST6GAL1 Clone 27. Furthermore, the total SA (mol/mol) in IgG produced by the enriched ST6GAL1 Clone 27 increased by 2-fold compared to the control. For host cell engineering, the CHOZN(®) GS host cell line was transfected and enriched for ST6GAL1 overexpression. Single-cell clones were derived from the enriched population and selected based on FITC-SNA staining and St6gal1 expression. Two clones ("ST6GAL1 OE Clone 31 and 32") were confirmed for the presence of α2,6-linked SA in total host cell protein extracts. ST6GAL1 OE Clone 32 was subsequently used to express SAFC human IgG1. The recombinant IgG expressed in this host cell line was confirmed to have α2,6-linked SA and increased total SA content. In conclusion, overexpression of St6gal1 is sufficient to produce recombinant proteins with increased sialylation and more human-like glycoprofiles without combinatorial engineering of other sialylation pathway genes. This work represents our ongoing effort of glycoengineering in CHO host cell lines for the development of "bio-better" protein therapeutics and cell culture vaccine production.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.