ArticleJournal of biomolecular NMR2015
Stable isotope labeling of glycoprotein expressed in silkworms using immunoglobulin G as a test molecule.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Glycoprotein Preparation by Heterologous Expression.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation.Biochemical Society transactions · 2022Review
- Structural insight and stability of TNFR-Fc fusion protein (Etanercept) produced by using transgenic silkworms.Journal of biochemistry · 2021Article
- Silkworm Pupae Function as Efficient Producers of Recombinant Glycoproteins with Stable-Isotope Labeling.Biomolecules · 2020Article
- Stable isotope labeling approaches for NMR characterization of glycoproteins using eukaryotic expression systems.Journal of biomolecular NMR · 2018Article
- NMR Detection of Semi-Specific Antibody Interactions in Serum Environments.Molecules (Basel, Switzerland) · 2017Article
Corrections and comments
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Authors and funding
13 authors at 8 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Silkworms serve as promising bioreactors for the production of recombinant proteins, including glycoproteins and membrane proteins, for structural and functional protein analyses. However, lack of methodology for stable isotope labeling has been a major deterrent to using this expression system for nuclear magnetic resonance (NMR) structural biology. Here we developed a metabolic isotope labeling technique using commercially available silkworm larvae. The fifth instar larvae were infected with baculoviruses for co-expression of recombinant human immunoglobulin G (IgG) as a test molecule, with calnexin as a chaperone. They were subsequently reared on an artificial diet containing (15)N-labeled yeast crude protein extract. We harvested 0.1 mg of IgG from larva with a (15)N-enrichment ratio of approximately 80%. This allowed us to compare NMR spectral data of the Fc fragment cleaved from the silkworm-produced IgG with those of an authentic Fc glycoprotein derived from mammalian cells. Therefore, we successfully demonstrated that our method enables production of isotopically labeled glycoproteins for NMR studies.
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