ArticlePlant physiology2008
Construction of a functional CMP-sialic acid biosynthesis pathway in Arabidopsis.
Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 80 citations in OpenAlex.
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- Engineered plants provide a photosynthetic platform for the production of diverse human milk oligosaccharides.Nature food · 2024Article
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- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Plant-derived VLP: a worthy platform to produce vaccine against SARS-CoV-2.Biotechnology letters · 2022Review
- Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Molecular Interactions of the Polysialytransferase Domain (PSTD) in ST8Sia IV with CMP-Sialic Acid and Polysialic Acid Required for Polysialylation of the Neural Cell Adhesion Molecule Proteins: An NMR Study.International journal of molecular sciences · 2020Article
- Stable Protein Sialylation in Physcomitrella.Frontiers in plant science · 2020Article
- Direct imaging of glycans in Arabidopsis roots via click labeling of metabolically incorporated azido-monosaccharides.BMC plant biology · 2016Article
- Biomanufacturing of protective antibodies and other therapeutics in edible plant tissues for oral applications.Plant biotechnology journal · 2016Review
- Engineering of complex protein sialylation in plants.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Transient Glyco-Engineering to Produce Recombinant IgA1 with Defined N- and O-Glycans in Plants.Frontiers in plant science · 2016Article
- Using GlycoDelete to produce proteins lacking plant-specific N-glycan modification in seeds.Nature biotechnology · 2015Article
- Limited Addition of the 6-Arm β1,2-linked N-Acetylglucosamine (GlcNAc) Residue Facilitates the Formation of the Largest N-Glycan in Plants.The Journal of biological chemistry · 2015Article
- Characterization of plants expressing the human β1,4-galactosyltrasferase gene.Plant physiology and biochemistry : PPB · 2015Article
- Article
- Proteolytic and N-glycan processing of human α1-antitrypsin expressed in Nicotiana benthamiana.Plant physiology · 2014Article
- Oligomerization status influences subcellular deposition and glycosylation of recombinant butyrylcholinesterase in Nicotiana benthamiana.Plant biotechnology journal · 2014Article
- Plant glyco-biotechnology on the way to synthetic biology.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have reported that plants contain negligible amounts of free or protein-bound N-acetylneuraminic acid (Neu5Ac). This is a major disadvantage for the use of plants as a biopharmaceutical expression system, since N-glycans with terminal Neu5Ac residues are important for the biological activities and half-lives of recombinant therapeutic glycoproteins in humans. For the synthesis of Neu5Ac-containing N-glycans, plants have to acquire the ability to synthesize Neu5Ac and its nucleotide-activated derivative, cytidine monophospho-N-acetylneuraminic acid. In this study, we have generated transgenic Arabidopsis (Arabidopsis thaliana) plants expressing three key enzymes of the mammalian Neu5Ac biosynthesis pathway: UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, N-acetylneuraminic acid phosphate synthase, and CMP-N-acetylneuraminic acid synthetase. Simultaneous expression of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase and N-acetylneuraminic acid phosphate synthase resulted in the generation of significant Neu5Ac amounts (1,275 nmol g(-1) fresh weight in leaves) in planta, which could be further converted to cytidine monophospho-N-acetylneuraminic acid (2.4 nmol g(-1) fresh weight in leaves) by coexpression of CMP-N-acetylneuraminic acid synthetase. These findings are a major step toward the production of Neu5Ac-containing glycoproteins in plants.
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