ArticlemAbs2019
Rapid production of a chimeric antibody-antigen fusion protein based on 2A-peptide cleavage and green fluorescent protein expression in CHO cells.
Article in mAbs, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- In silico design and validation of a Plasmodium falciparum multi-epitope diagnostic antigen (PfMEDA1) for the diagnosis of falciparum malaria.BMC infectious diseases · 2025Article
- Uptake and nuclear translocation of lactoferrin by porcine monocytes: impact of iron binding, protease activity, and monocyte activation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Article
- Does a Polycistronic 2A Design Enable Functional FcRn Production for Antibody Pharmacokinetic Studies?Pharmaceutics · 2025Article
- Construction of an Integration Vector with a Chimeric Signal Peptide for the Expression of Monoclonal Antibodies in Mammalian Cells.Current issues in molecular biology · 2024Article
- Targeted delivery of oral vaccine antigens to aminopeptidase N protects pigs against pathogenicFrontiers in immunology · 2023Article
- Lactoferrin Decreases EnterotoxigenicPharmaceutics · 2022Article
- Strategies and Considerations for Improving Recombinant Antibody Production and Quality in Chinese Hamster Ovary Cells.Frontiers in bioengineering and biotechnology · 2022Review
- Expression of antibody fragments in Saccharomyces cerevisiae strains evolved for enhanced protein secretion.Microbial cell factories · 2021Article
- Antibody-Mediated Targeting of Antigens to Intestinal Aminopeptidase N Elicits Gut IgA Responses in Pigs.Frontiers in immunology · 2021Article
- Porcine and Bovine Forms of Lactoferrin Inhibit Growth of Porcine Enterotoxigenic Escherichia coli and Degrade Its Virulence Factors.Applied and environmental microbiology · 2020Article
- The Intriguing Interaction of Escherichia coli with the Host Environment and Innovative Strategies To Interfere with Colonization: a Summary of the 2019 E. coli and the Mucosal Immune System Meeting.Applied and environmental microbiology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To enable large-scale antibody production, the creation of a stable, high producer cell line is essential. This process often takes longer than 6 months using standard limited dilution techniques and is very labor intensive. The use of a tri-cistronic vector expressing green fluorescent protein (GFP) and both antibody chains, separated by a GT2A peptide sequence, allows expression of all proteins under a single promotor in equimolar ratios. By combining the advantages of 2A peptide cleavage and single cell sorting, a chimeric antibody-antigen fusion protein that contained the variable domains of mouse IgG with a porcine IgA constant domain fused to the FedF antigen could be produced in CHO-K1 cells. After transfection, a strong correlation was found between antibody production and GFP expression (r = 0.69) using image analysis of formed monolayer patches. This enables the rapid selection of GFP-positive clones using automated image analysis for the selection of high producer clones. This vector design allowed the rapid selection of high producer clones within a time-frame of 4 weeks after transfection. The highest producing clone had a specific antibody productivity of 2.32 pg/cell/day. Concentrations of 34 mg/L were obtained using shake-flask batch culture. The produced recombinant antibody showed stable expression, binding and minimal degradation. In the future, this antibody will be assessed for its effectiveness as an oral vaccine antigen.
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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.