Evidence map›Paper›PMID 25689888›Full record

ArticlePlant cell reports2015

NMR-based structural validation of therapeutic antibody produced in Nicotiana benthamiana.

Hirokazu Yagi, Noriho Fukuzawa, Yasushi Tasaka, Kouki Matsuo, Ying Zhang, Takumi Yamaguchi, Sachiko Kondo, Shiori Nakazawa, Noritaka Hashii, Nana Kawasaki and 2 more

Abstract read
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Article in Plant cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.3field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Glycoprotein Preparation by Heterologous Expression.Methods in molecular biology (Clifton, N.J.) · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 7 institutions in 1 country.

Hirokazu YagiFaculty and Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan.
Noriho Fukuzawa
Yasushi Tasaka
Kouki Matsuo
Ying Zhang
Takumi Yamaguchi
Sachiko Kondo
Shiori Nakazawa
Noritaka Hashii
Nana Kawasaki
Takeshi Matsumura
Koichi Kato
National Institute of Advanced Industrial Science and Technology · JPNagoya City University · JPNational Institute of Health Sciences · JPInstitute for Molecular Science · JPNagoya University · JPOchanomizu University · JPOkazaki Institute for Integrative Bioscience · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

key messageWe successfully developed a method for metabolic isotope labeling of recombinant proteins produced in transgenic tobacco. This enabled assessment of structural integrity of plant-derived therapeutic antibodies by NMR analysis. A variety of expression vehicles have been developed for the production of promising biologics, including plants, fungi, bacteria, insects, and mammals. Glycoprotein biologics often experience altered folding and post-translational modifications that are typified by variant glycosylation patterns. These differences can dramatically affect their efficacy, as exemplified by therapeutic antibodies. However, it is generally difficult to validate the structural integrity of biologics produced using different expression vehicles. To address this issue, we have developed and applied a stable-isotope-assisted nuclear magnetic resonance (NMR) spectroscopy method for the conformational characterization of recombinant antibodies produced in plants. Nicotiana benthamiana used as a vehicle for the production of recombinant immunoglobulin G (IgG) was grown in a (15)N-enriched plant growth medium. The Fc fragment derived from the (15)N-labeled antibody thus prepared was subjected to heteronuclear two-dimensional (2D) NMR measurements. This approach enabled assessment of the structural integrity of the plant-derived therapeutic antibodies by comparing their NMR spectral properties with those of an authentic IgG-Fc derived from mammalian cells.

Indexed as

AdalimumabAmino Acid SequenceCarbohydrate SequenceGlycosylationImmunoglobulin Fc FragmentsImmunoglobulin GMolecular Sequence DataNicotianaNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPlants, Genetically ModifiedRecombinant ProteinsReproducibility of ResultsAdalimumabImmunoglobulin Fc FragmentsImmunoglobulin GNitrogen IsotopesRecombinant Proteins

Identifiers

PMID25689888
OpenAlexW2095463140

What OpenQuestion holds

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Registered trials

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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.