ArticleJournal of proteome research2017
Exploring Site-Specific N-Glycosylation of HEK293 and Plant-Produced Human IgA Isotypes.
Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 52 citations in OpenAlex.
- Vectored Immunoprophylaxis for Mucosal Immunity: Advances and Challenges Associated with Recombinant Secretory IgA Expression.Vaccines · 2026Review
- IgA binding characteristics of golden hamster and ferret Fcα receptors.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- The Production and Purification of Therapeutic Antibodies: A Comprehensive Analysis of Process- and Product-Related Contaminants.Biomolecules · 2026Review
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Enhancing quality and yield of recombinant secretory IgA antibodies in Nicotiana benthamiana by endoplasmic reticulum engineering.Plant biotechnology journal · 2025Article
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- Production of recombinant IgA1 with defined mucin-type O-glycans inFrontiers in plant science · 2025Article
- AsymmetricJournal of the American Chemical Society · 2024Article
- Stability Engineering of Recombinant Secretory IgA.International journal of molecular sciences · 2024Article
- Recombinant neutralizing secretory IgA antibodies for preventing mucosal acquisition and transmission of SARS-CoV-2.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- A genome-edited N. benthamiana line for industrial-scale production of recombinant glycoproteins with targeted N-glycosylation.Biotechnology journal · 2024Article
- Improving theFrontiers in plant science · 2024Article
- Implications of O-glycan modifications in the hinge region of a plant-produced SARS-CoV-2-IgA antibody on functionality.Frontiers in bioengineering and biotechnology · 2024Article
- Engineered Secretory Immunoglobulin A provides insights on antibody-based effector mechanisms targetingbioRxiv : the preprint server for biology · 2023Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- IgA antibody immunotherapy targeting GD2 is effective in preclinical neuroblastoma models.Journal for immunotherapy of cancer · 2023Article
- An oligosaccharyltransferase fromFrontiers in plant science · 2023Article
- Review
- Investigation of theMolecules (Basel, Switzerland) · 2022Article
- Transient Expression of Glycosylated SARS-CoV-2 Antigens inPlants (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The full potential of recombinant Immunoglobulin A as therapeutic antibody is not fully explored, owing to the fact that structure-function relationships of these extensively glycosylated proteins are not well understood. Here monomeric IgA1, IgA2m(1), and IgA2m(2) variants of the anti-HER2 antibody (IgG1) trastuzumab were expressed in glyco-engineered Nicotiana benthamiana plants and in human HEK293-6E cells. All three IgA isotypes were purified and subjected to biophysical and biochemical characterization. While no differences in assembly, antigen binding, and glycosylation occupancy were observed, both systems vary tremendously in terms of glycan structures and heterogeneity of glycosylation. Mass-spectrometric analysis of site-specific glycosylation revealed that plant-produced IgAs carry mainly complex-type biantennary N-glycans. HEK293-6E-produced IgAs, on the contrary, showed very heterogeneous N-glycans with high levels of sialylation, core-fucose, and the presence of branched structures. The site-specific analysis revealed major differences between the individual N-glycosylation sites of each IgA subtype. Moreover, the proline-rich hinge region from HEK293-6E cell-derived IgA1 was occupied with mucin-type O-glycans, whereas IgA1 from N. benthamiana displayed numerous plant-specific modifications. Interestingly, a shift in unfolding of the CH2 domain of plant-produced IgA toward lower temperatures can be observed with differential scanning calorimetry, suggesting that distinct glycoforms affect the thermal stability of IgAs.
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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.