The University of Osaka · Biochemistry, Genetics and Molecular Biology
Professor Kazuhito Fujiyama's research lab specializes in plant molecular biology and biotechnology, with a primary focus on glyco-engineering of plants for the production of therapeutic proteins. The lab investigates plant-specific N-glycan structures—particularly β1,2-xylose and core α1,3-fucose—and develops genetic tools, such as RNAi, to eliminate these immunogenic modifications. A key achievement includes creating glyco-engineered Nicotiana benthamiana plants with predominantly high-mannose glycans, ideal for producing safe, human-compatible glycoproteins. The lab also explores the post-translational modification of recombinant proteins, exemplified by the production and structural analysis of human lactoferrin in transgenic rice.
Figures are computed from collected data and may differ slightly.
We have isolated, cloned and characterized three cDNAs and two genomic DNAs corresponding to the mRNAs and genes for the horseradish (Armoracia rusticana) peroxidase isoenzyme C (HPR C). The amino acid sequence of HRP C1, deduced from the nucleotide sequence of one of the cDNA clone, pSK1, contained the same primary sequence as that of the purified enzyme established by Welinder [FEBS Lett. 72, 19-23 (1976)] with additional sequences at the N and C terminal. All three inserts in the cDNA clones,
For the production of therapeutic proteins in plants, the presence of β1,2-xylose and core α1,3-fucose on plants' N-glycan structures has been debated for their antigenic activity. In this study, RNA interference (RNAi) technology was used to down-regulate the endogenous N-acetylglucosaminyltransferase I (GNTI) expression in Nicotiana benthamiana. One glyco-engineered line (NbGNTI-RNAi) showed a strong reduction of plant-specific N-glycans, with the result that as much as 90.9% of the total N-gl
Human lactoferrin was produced in genetically engineered rice. N-linked glycan structures of recombinant human lactoferrin were determined. The oligosaccharides liberated by hydrazinolysis were labeled with 2-aminopyridine (PA). The PA-labeled glycans were purified by reverse-phase and size-fractionation HPLCs. The structures of these glycans were identified by HPLC, exoglycosidase digestion, and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The glycan
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