ArticleBiotechnology progress2020
Highly sensitive HPLC analysis and biophysical characterization of N-glycans of IgG-Fc domain in comparison between CHO and 293 cells using FcγRIIIa ligand.
Article in Biotechnology progress, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 6 citations in OpenAlex.
- Pairing of high-mannose glycans in human IgE-Fc: implications for secretion and stability.Clinical proteomics · 2026Article
- Mitigating alkaline instability induced by tyrosine-tyrosine repulsion in an FcγRIIIa-binding protein through phenylalanine substitution.Journal of biochemistry · 2026Article
- Current Landscape and Future Directions in Cancer Immunotherapy: Therapies, Trials, and Challenges.Cancers · 2025Review
- Application of the iPLUS non-coding sequence in improving biopharmaceuticals production.Frontiers in bioengineering and biotechnology · 2024Article
- Biophysical Characterization of the Contribution of the Fab Region to the IgG-FcγRIIIa Interaction.Biochemistry · 2023Article
- Codon optimization regulates IgG3 and IgM expression and glycosylation inFrontiers in bioengineering and biotechnology · 2023Article
- Improvement of the affinity of an anti-rat P2X4 receptor antibody by introducing electrostatic interactions.Scientific reports · 2022Article
- Highly sensitive HPLC analysis and biophysical characterization of N-glycans of IgG-Fc domain in comparison between CHO and 293 cells using FcγRIIIa ligand.Biotechnology progress · 2020Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Quality control of monoclonal antibodies is challenging due in part to the diversity of post-translational modifications present. The regulation of the N-glycans of IgG-Fc domain is one of the key factors to maintain the safety and efficacy of antibody drugs. The FcγRIIIa affinity column is an attractive tool for the precise analysis of the N-glycans in IgG-Fc domain. We used the mutant FcγRIIIa, which is produced in Escherichia coli and is therefore not glycosylated, as an affinity reagent to analyze the N-glycans of monoclonal antibodies expressed in Expi293 and ExpiCHO cells. The monoclonal antibodies expressed in these cells showed very different chromatograms, because of differences in terminal galactose residues on the IgG-Fc domains. We also carried out kinetic and thermodynamic analyses to understand the interaction between monoclonal antibodies and the mutant FcγRIIIa. Expi293 cell-derived monoclonal antibodies had higher affinity for the mutant FcγRIIIa than those derived from ExpiCHO cells, due to slower off rates and lower binding entropy loss. Collectively, our results suggest that the FcγRIIIa column can be used to analyze the glycosylation of antibodies rapidly and specifically.
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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.