ArticlemAbs2015
Production of α2,6-sialylated IgG1 in CHO cells.
Article in mAbs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 101 citations in OpenAlex.
- Separation of Monoclonal Antibody Aggregates Using an Analytical Ultrafiltration Technique.Membranes · 2026Article
- Integrating text mining and knowledge graph to enhance biopharmaceutical process optimization.PloS one · 2026Article
- Identification of new fucosyltransferase-8 inhibitors: An integrated biochemical, biophysical, and computational approach.PloS one · 2026Article
- The anti-inflammatory activity of IgG is enhanced by co-engagement of type I and II Fc receptors.Science (New York, N.Y.) · 2025Article
- A Surface Plasmon Resonance-Based Integrated Assay for Quantification and Glycosylation Characterization of Monoclonal Antibodies in Crude Heterogeneous Samples.Biotechnology and bioengineering · 2025Article
- Use of Coiled-Coil Affinity Peptides to Manufacture Antibody Conjugates.Bioconjugate chemistry · 2025Article
- MiRNA Chaining for Efficient Stable Overexpression to Improve Protein Quantity and Quality in CHO Cells.Methods in molecular biology (Clifton, N.J.) · 2025Article
- A Novel Antigen Design Strategy to Isolate Single-Domain Antibodies that Target Human Nav1.7 and Reduce Pain in Animal Models.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Stable overexpression of native and artificial miRNAs for the production of differentially fucosylated antibodies in CHO cells.Engineering in life sciences · 2024Article
- Combinatory glycoengineering of monoclonal antibodies and its application in cancer therapy: a narrative review.Translational cancer research · 2024Review
- An engineered immunomodulatory IgG1 Fc suppresses autoimmune inflammation through pathways shared with i.v. immunoglobulin.The Journal of clinical investigation · 2024Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Optimizing effector functions of monoclonal antibodies via tailored N-glycan engineering using a dual landing pad CHO targeted integration platform.Scientific reports · 2023Article
- Cell factory engineering: Challenges and opportunities for synthetic biology applications.Biotechnology and bioengineering · 2023Review
- Production of recombinant human IgG1 Fc with beneficial N-glycosylation pattern for anti-inflammatory activity using genome-edited chickens.Communications biology · 2023Article
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Fragmentation stability and retention time-shift obtained by LC-MS/MS to distinguish sialylatedJournal of pharmaceutical analysis · 2023Article
- Producing Biologics with Defined N-Glycosylation in Plants.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Glycoconjugates: Synthesis, Functional Studies, and Therapeutic Developments.Chemical reviews · 2022Review
- Sialylation as an Important Regulator of Antibody Function.Frontiers in immunology · 2022Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence of α2,6-sialic acids on the Fc N-glycan provides anti-inflammatory properties to the IgGs through a mechanism that remains unclear. Fc-sialylated IgGs are rare in humans as well as in industrial host cell lines such as Chinese hamster ovary (CHO) cells. Facilitated access to well-characterized α2,6-sialylated IgGs would help elucidate the mechanism of this intriguing IgG's effector function. This study presents a method for the efficient Fc glycan α2,6-sialylation of a wild-type and a F243A IgG1 mutant by transient co-expression with the human α2,6-sialyltransferase 1 (ST6) and β1,4-galactosyltransferase 1 (GT) in CHO cells. Overexpression of ST6 alone only had a moderate effect on the glycoprofiles, whereas GT alone greatly enhanced Fc-galactosylation, but not sialylation. Overexpression of both GT and ST6 was necessary to obtain a glycoprofile dominated by α2,6-sialylated glycans in both antibodies. The wild-type was composed of the G2FS(6)1 glycan (38%) with remaining unsialylated glycans, while the mutant glycoprofile was essentially composed of G2FS(6)1 (25%), G2FS(3,6)2 (16%) and G2FS(6,6)2 (37%). The α2,6-linked sialic acids represented over 85% of all sialic acids in both antibodies. We discuss how the limited sialylation level in the wild-type IgG1 expressed alone or with GT results from the glycan interaction with Fc's amino acid residues or from intrinsic galactosyl- and sialyl-transferases substrate specificities.
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Registered trials
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.