ArticlemAbs
High level expression of functional human IgMs in human PER.C6 cells.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 61 citations in OpenAlex.
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Article
- Animal Cell Lines as Expression Platforms in Viral Vaccine Production: A Post Covid-19 Perspective.ACS omega · 2024Review
- Article
- Conjugated detergent micelles as a platform for IgM purification.Biotechnology and bioengineering · 2022Article
- Sialylation as an Important Regulator of Antibody Function.Frontiers in immunology · 2022Review
- Structure, Function, and Therapeutic Use of IgM Antibodies.Antibodies (Basel, Switzerland) · 2020Review
- Transient pentameric IgM fulfill biological function-Effect of expression host and transfection on IgM properties.PloS one · 2020Article
- The role of magnetic field in the biopharmaceutical production: Current perspectives.Biotechnology reports (Amsterdam, Netherlands) · 2019Review
- An IgM antibody targeting the receptor binding site of influenza B blocks viral infection with great breadth and potency.Theranostics · 2019Article
- Identification of Novel Epitopes with Agonistic Activity for the Development of Tumor Immunotherapy Targeting TRAIL-R1.Journal of Cancer · 2017Article
- Site-Specific N-Glycosylation of Recombinant Pentameric and Hexameric Human IgM.Journal of the American Society for Mass Spectrometry · 2016Article
- TRAIL-receptor 1 IgM antibodies strongly induce apoptosis in human cancer cells in vitro and in vivo.Oncoimmunology · 2016Article
- Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM.Biochimica et biophysica acta · 2015Article
- Harnessing the fcμ receptor for potent and selective cytotoxic therapy of chronic lymphocytic leukemia.Cancer research · 2014Article
- Elastin-like polypeptides as a promising family of genetically-engineered protein based polymers.World journal of microbiology & biotechnology · 2014Review
- Designed IgM from glycoengineering.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Expression and glycoengineering of functionally active heteromultimeric IgM in plants.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Identification of host-immune response protein candidates in the sera of human oral squamous cell carcinoma patients.PloS one · 2014Article
- Simultaneous binding of the anti-cancer IgM monoclonal antibody PAT-SM6 to low density lipoproteins and GRP78.PloS one · 2013Article
Corrections and comments
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Authors and funding
16 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Natural IgM antibodies play an important role in the body's defense mechanisms against transformed cells in the human body and are currently being exploited both in prognoses of malignant lesions and in the therapy of cancer patients. However, despite growing interest and clinical promise, thus far the IgM class of antibodies has failed to gain widespread commercial interest as these are considered to be difficult to produce recombinantly. IgMs are polymeric and have a relatively large mass. In addition, IgM molecules are heavily glycosylated and, when produced in non-human cell lines, they may contain non-human glycan structures which may be potentially immunogenic. Clearly, production systems capable of expressing human recombinant IgM antibodies are needed. We have successfully used PER.C6 cells-a human cell line-to generate three separate human recombinant monoclonal IgMs in suspension cultures in protein-free medium. All three of the IgMs were constructed with joining (J) chain and were expressed in the pentameric form. One of the IgMs was also expressed as a hexamer without J chain. Clones with cell specific productivities greater than 20 pg/cell/day were generated, which led to yields of 0.5 g/L to 2g/L in fed-batch production. All the IgMs expressed were biologically active as shown in binding and cytotoxicity assays. These studies demonstrate the potential of PER.C6 cells for the production of high levels of functional recombinant IgM and other polymeric molecules, using a straightforward and rapid stable cell line generation method.
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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.