ArticleThe Journal of biological chemistry2012
Engineering of sialylated mucin-type O-glycosylation in plants.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 92 citations in OpenAlex.
- Polysialic Acid Synthesis on theACS omega · 2026Article
- Identification of β-galactosidases along the secretory pathway of Nicotiana benthamiana that collectively hamper engineering of galactose-extended glycans on recombinant glycoproteins.Plant biotechnology journal · 2026Article
- 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
- Production of recombinant IgA1 with defined mucin-type O-glycans inFrontiers in plant science · 2025Article
- Fine-tuning the N-glycosylation of recombinant human erythropoietin using Chlamydomonas reinhardtii mutants.Plant biotechnology journal · 2024Article
- Plant-made pharmaceuticals.Plant biotechnology (Tokyo, Japan) · 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
- Green Biologics: Harnessing the Power of Plants to Produce Pharmaceuticals.International journal of molecular sciences · 2023Review
- Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023Review
- 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
- Glyco-Engineering Plants to Produce Helminth Glycoproteins as Prospective Biopharmaceuticals: Recent Advances, Challenges and Future Prospects.Frontiers in plant science · 2022Review
- Frontiers in the Standardization of the Plant Platform for High Scale Production of Vaccines.Plants (Basel, Switzerland) · 2021Review
- Review
- Go your own way: membrane-targeting sequences.Plant physiology · 2021Article
- Prolyl Hydroxylase Paralogs inFrontiers in plant science · 2021Article
- In Planta Production of the Receptor-Binding Domain From SARS-CoV-2 With Human Blood Group A Glycan Structures.Frontiers in chemistry · 2021Article
- Editorial: Plant Glycobiology - A Sweet World of Glycans, Glycoproteins, Glycolipids, and Carbohydrate-Binding Proteins.Frontiers in plant science · 2021Article
- Plant Platforms for Efficient Heterologous Protein Production.Biotechnology and bioprocess engineering : BBE · 2021Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Proper N- and O-glycosylation of recombinant proteins is important for their biological function. Although the N-glycan processing pathway of different expression hosts has been successfully modified in the past, comparatively little attention has been paid to the generation of customized O-linked glycans. Plants are attractive hosts for engineering of O-glycosylation steps, as they contain no endogenous glycosyltransferases that perform mammalian-type Ser/Thr glycosylation and could interfere with the production of defined O-glycans. Here, we produced mucin-type O-GalNAc and core 1 O-linked glycan structures on recombinant human erythropoietin fused to an IgG heavy chain fragment (EPO-Fc) by transient expression in Nicotiana benthamiana plants. Furthermore, for the generation of sialylated core 1 structures constructs encoding human polypeptide:N-acetylgalactosaminyltransferase 2, Drosophila melanogaster core 1 β1,3-galactosyltransferase, human α2,3-sialyltransferase, and Mus musculus α2,6-sialyltransferase were transiently co-expressed in N. benthamiana together with EPO-Fc and the machinery for sialylation of N-glycans. The formation of significant amounts of mono- and disialylated O-linked glycans was confirmed by liquid chromatography-electrospray ionization-mass spectrometry. Analysis of the three EPO glycopeptides carrying N-glycans revealed the presence of biantennary structures with terminal sialic acid residues. Our data demonstrate that N. benthamiana plants are amenable to engineering of the O-glycosylation pathway and can produce well defined human-type O- and N-linked glycans on recombinant therapeutics.
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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.