ArticleProceedings of the National Academy of Sciences of the United States of America2014
Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 79 citations in OpenAlex.
- Plant-Based Systems for Producing Therapeutic Proteins: Current Status and Future Prospects.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Fc Profiling of Polyclonal IgG, IgA and IgM by Light Chain Capturing Coupled with NanoRP-LC-MS.JACS Au · 2026Article
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026Review
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- Not All Arms of IgM Are Equal: Following Hinge-Directed Cleavage by Online Native SEC-Orbitrap-Based CDMS.Journal of the American Society for Mass Spectrometry · 2024Article
- IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition.Nature communications · 2024Article
- Article
- A genome-edited N. benthamiana line for industrial-scale production of recombinant glycoproteins with targeted N-glycosylation.Biotechnology journal · 2024Article
- Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023Review
- Codon optimization regulates IgG3 and IgM expression and glycosylation inFrontiers in bioengineering and biotechnology · 2023Article
- An oligosaccharyltransferase fromFrontiers in plant science · 2023Article
- Glyco engineered pentameric SARS-CoV-2 IgMs show superior activities compared to IgG1 orthologues.Frontiers in immunology · 2023Article
- Impact of glycoengineering and antidrug antibodies on the anticancer activity of a plant-made lectin-Fc fusion protein.Plant biotechnology journal · 2022Article
- Development of plant-made monoclonal antibodies against viral infections.Current opinion in virology · 2022Review
- Humanization and expression of IgG and IgM antibodies in plants as potential diagnostic reagents for Valley Fever.Frontiers in plant science · 2022Article
- Increased in vitro neutralizing activity of SARS-CoV-2 IgA1 dimers compared to monomers and IgG.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis.Experientia supplementum (2012) · 2021Article
- Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics. Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet. Plants have a proven record for the production of therapeutically relevant recombinant proteins. However, whether they are able to express proteins like IgM antibodies, which range among the most complex human proteins, remains unknown so far. Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6). SM6 efficiently accumulates in plant leaves and assembles correctly into heterooligomers (pentamers and hexamers). Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6. Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM. A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation. Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts. The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications. Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
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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.