Evidence map›Paper›PMID 17227846›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds.

Bart Van Droogenbroeck, Jingyuan Cao, Johannes Stadlmann, Friedrich Altmann, Sarah Colanesi, Stefan Hillmer, David G Robinson, Els Van Lerberge, Nancy Terryn, Marc Van Montagu and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

43 citing papers in PubMed, 120 citations in OpenAlex.

  1. Review
  2. Review
  3. Cell Biology Methods to Study Recombinant Proteins in Seeds.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  4. Review
  5. Plant Platforms for Efficient Heterologous Protein Production.Biotechnology and bioprocess engineering : BBE · 2021
    Review
  6. Article
  7. Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
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  18. Review
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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

13 authors at 6 institutions in 4 countries.

Bart Van DroogenbroeckDepartment of Plant Systems Biology, Flanders Interuniversity Institute for Biotechnology, Ghent University, Technologiepark 927, B-9052 Ghent, Belgium.
Jingyuan Cao
Johannes Stadlmann
Friedrich Altmann
Sarah Colanesi
Stefan Hillmer
David G Robinson
Els Van Lerberge
Nancy Terryn
Marc Van Montagu
Mifang Liang
Ann Depicker
Geert De Jaeger
Ghent University · BEHeidelberg University · DEBOKU University · ATVlaams Instituut voor Biotechnologie · BENational Institute for Viral Disease Control and Prevention · CNVIB - International Plant Biotechnology Outreach · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Production of high-value recombinant proteins in transgenic seeds is an attractive and economically feasible alternative to conventional systems based on mammalian cells and bacteria. In contrast to leaves, seeds allow high-level accumulation of recombinant proteins in a relatively small volume and a stable environment. We demonstrate that single-chain variable fragment (scFv)-Fc antibodies, with N-terminal signal sequence and C-terminal KDEL tag, can accumulate to very high levels as bivalent IgG-like antibodies in Arabidopsis thaliana seeds and illustrate that a plant-produced anti-hepatitis A virus scFv-Fc has similar antigen-binding and in vitro neutralizing activities as the corresponding full-length IgG. As expected, most scFv-Fc produced in seeds contained only oligomannose-type N-glycans, but, unexpectedly, 35-40% was never glycosylated. A portion of the scFv-Fc was found in endoplasmic reticulum (ER)-derived compartments delimited by ribosome-associated membranes. Additionally, consistent with the glycosylation data, large amounts of the recombinant protein were deposited in the periplasmic space, implying a direct transport from the ER to the periplasmic space between the plasma membrane and the cell wall. Aberrant localization of the ER chaperones calreticulin and binding protein (BiP) and the endogenous seed storage protein cruciferin in the periplasmic space suggests that overproduction of recombinant scFv-Fc disturbs normal ER retention and protein-sorting mechanisms in the secretory pathway.

Indexed as

ArabidopsisElectrophoresis, Polyacrylamide GelGlycosylationMass SpectrometryMicroscopy, ElectronPeptide MappingPlantibodiesPlants, Genetically ModifiedTrypsinPlantibodiesTrypsin

Identifiers

PMID17227846
PMCPMC1783127
OpenAlexW2124111803

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.