ArticleFrontiers in plant science2016
Transient Glyco-Engineering to Produce Recombinant IgA1 with Defined N- and O-Glycans in Plants.
Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 69 citations in OpenAlex.
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- 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
- An oligosaccharyltransferase fromFrontiers in plant science · 2023Article
- Three Parts of the Plant Genome: On the Way to Success in the Production of Recombinant Proteins.Plants (Basel, Switzerland) · 2022Review
- Transient Expression of Glycosylated SARS-CoV-2 Antigens inPlants (Basel, Switzerland) · 2022Review
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Engineering theFrontiers in plant science · 2022Article
- Glyco-Engineering Plants to Produce Helminth Glycoproteins as Prospective Biopharmaceuticals: Recent Advances, Challenges and Future Prospects.Frontiers in plant science · 2022Review
- Targeted genome editing of plants and plant cells for biomanufacturing.Transgenic research · 2021Review
- Leaf infiltration in plant science: old method, new possibilities.Plant methods · 2021Review
- Plant-derived secretory component gives protease-resistance to Shiga toxin 1-specific dimeric IgA.Plant molecular biology · 2021Article
- Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Immunoglobulin A Glycosylation and Its Role in Disease.Experientia supplementum (2012) · 2021Article
- Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021Article
- Site-Specific Glycosylation of Recombinant Viral Glycoproteins Produced inFrontiers in plant science · 2021Article
- Fc Engineering Strategies to Advance IgA Antibodies as Therapeutic Agents.Antibodies (Basel, Switzerland) · 2020Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Monitoring of immunoglobulin N- and O-glycosylation in health and disease.Glycobiology · 2020Review
- In-depth characterization of Trichoderma reesei cellobiohydrolase TrCel7A produced in Nicotiana benthamiana reveals limitations of cellulase production in plants by host-specific post-translational modifications.Plant biotechnology journal · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The production of therapeutic antibodies to combat pathogens and treat diseases, such as cancer is of great interest for the biotechnology industry. The recent development of plant-based expression systems has demonstrated that plants are well-suited for the production of recombinant monoclonal antibodies with defined glycosylation. Compared to immunoglobulin G (IgG), less effort has been undertaken to express immunoglobulin A (IgA), which is the most prevalent antibody class at mucosal sites and a promising candidate for novel recombinant biopharmaceuticals with enhanced anti-tumor activity. Here, we transiently expressed recombinant human IgA1 against the VP8* rotavirus antigen in glyco-engineered ΔXT/FT Nicotiana benthamiana plants. Mass spectrometric analysis of IgA1 glycopeptides revealed the presence of complex biantennary N-glycans with terminal N-acetylglucosamine present on the N-glycosylation site of the CH2 domain in the IgA1 alpha chain. Analysis of the peptide carrying nine potential O-glycosylation sites in the IgA1 alpha chain hinge region showed the presence of plant-specific modifications including hydroxyproline formation and the attachment of pentoses. By co-expression of enzymes required for initiation and elongation of human O-glycosylation it was possible to generate disialylated mucin-type core 1 O-glycans on plant-produced IgA1. Our data demonstrate that ΔXT/FT N. benthamiana plants can be engineered toward the production of recombinant IgA1 with defined human-type N- and O-linked glycans.
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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.