ArticleThe Journal of biological chemistry2012
Engineering mammalian 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 35 papers.
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Who cites it
35 citing papers in PubMed, 63 citations in OpenAlex.
- Cross-talk between glycosylation pathways: Mechanistic insights and implications for human diseases.Molecular metabolism · 2026Review
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Tetraspanin CD82 regulates transforming growth factor-β signaling in hematopoietic stem and progenitor cells.Molecular biology of the cell · 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
- 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
- Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023Review
- Transient Expression of Glycosylated SARS-CoV-2 Antigens inPlants (Basel, Switzerland) · 2022Review
- Glyco-Engineering Plants to Produce Helminth Glycoproteins as Prospective Biopharmaceuticals: Recent Advances, Challenges and Future Prospects.Frontiers in plant science · 2022Review
- β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021Article
- Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021Article
- Prolyl Hydroxylase Paralogs inFrontiers in plant science · 2021Article
- Engineering orthogonal human O-linked glycoprotein biosynthesis in bacteria.Nature chemical biology · 2020Article
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Review
- A Roadmap for the Molecular Farming of Viral Glycoprotein Vaccines: Engineering Glycosylation and Glycosylation-Directed Folding.Frontiers in plant science · 2020Review
- Advanced Plant-Based Glycan Engineering.Frontiers in bioengineering and biotechnology · 2018Review
- Transient co-expression with threePlant methods · 2018Article
- Exploring Site-Specific N-Glycosylation of HEK293 and Plant-Produced Human IgA Isotypes.Journal of proteome research · 2017Article
- Production and glyco-engineering of immunomodulatory helminth glycoproteins in plants.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mucin-type O-glycosylation is an important post-translational modification that confers a variety of biological properties and functions to proteins. This post-translational modification has a particularly complex and differentially regulated biosynthesis rendering prediction and control of where O-glycans are attached to proteins, and which structures are formed, difficult. Because plants are devoid of GalNAc-type O-glycosylation, we have assessed requirements for establishing human GalNAc O-glycosylation de novo in plants with the aim of developing cell systems with custom-designed O-glycosylation capacity. Transient expression of a Pseudomonas aeruginosa Glc(NAc) C4-epimerase and a human polypeptide GalNAc-transferase in leaves of Nicotiana benthamiana resulted in GalNAc O-glycosylation of co-expressed human O-glycoprotein substrates. A chimeric YFP construct containing a 3.5 tandem repeat sequence of MUC1 was glycosylated with up to three and five GalNAc residues when co-expressed with GalNAc-T2 and a combination of GalNAc-T2 and GalNAc-T4, respectively, as determined by mass spectrometry. O-Glycosylation was furthermore demonstrated on a tandem repeat of MUC16 and interferon α2b. In plants, prolines in certain classes of proteins are hydroxylated and further substituted with plant-specific O-glycosylation; unsubstituted hydroxyprolines were identified in our MUC1 construct. In summary, this study demonstrates that mammalian type O-glycosylation can be established in plants and that plants may serve as a host cell for production of recombinant O-glycoproteins with custom-designed O-glycosylation. The observed hydroxyproline modifications, however, call for additional future engineering efforts.
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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.