Evidence map›Paper›PMID 31956981›Full record

ArticleBiotechnology and bioengineering2020

Plant-derived protein bodies as delivery vehicles for recombinant proteins into mammalian cells.

Jennifer Schwestka, Marc Tschofen, Stefan Vogt, Sylvain Marcel, Johannes Grillari, Marianne Raith, Ines Swoboda, Eva Stoger

Open access · hybridAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Vaccines · 2025
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023
    Review
  8. Generation of multi-layered protein bodies inFrontiers in plant science · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
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

8 authors at 3 institutions in 1 country.

Jennifer SchwestkaDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Marc TschofenDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Stefan VogtDepartment of Biotechnology, Institute of Molecular Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
Sylvain MarceliBio CDMO, Bryan, Texas.
Johannes GrillariDepartment of Biotechnology, Institute of Molecular Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
Marianne RaithBiotechnology Section, FH Campus Wien, University of Applied Sciences Campus Vienna Biocenter, Vienna, Austria.
Ines SwobodaBiotechnology Section, FH Campus Wien, University of Applied Sciences Campus Vienna Biocenter, Vienna, Austria.
Eva StogerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0002-7651-7992
BOKU University · ATHochschule Campus Wien · ATInstitute of Molecular Biotechnology · AT

Funding

Austrian Science Fund W1224Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

The encapsulation of biopharmaceuticals into micro- or nanoparticles is a strategy frequently used to prevent degradation or to achieve the slow release of therapeutics and vaccines. Protein bodies (PBs), which occur naturally as storage organelles in seeds, can be used as such carrier vehicles. The fusion of the N-terminal sequence of the maize storage protein, γ-zein, to other proteins is sufficient to induce the formation of PBs, which can be used to bioencapsulate recombinant proteins directly in the plant production host. In addition, the immunostimulatory effects of zein have been reported, which are advantageous for vaccine delivery. However, little is known about the interaction between zein PBs and mammalian cells. To better understand this interaction, fluorescent PBs, resulting from the fusion of the N-terminal portion of zein to a green fluorescent protein, was produced in Nicotiana benthamiana leaves, recovered by a filtration-based downstream procedure, and used to investigate their internalization efficiency into mammalian cells. We show that fluorescent PBs were efficiently internalized into intestinal epithelial cells and antigen-presenting cells (APCs) at a higher rate than polystyrene beads of comparable size. Furthermore, we observed that PBs stimulated cytokine secretion by epithelial cells, a characteristic that may confer vaccine adjuvant activities through the recruitment of APCs. Taken together, these results support the use of zein fusion proteins in developing novel approaches for drug delivery based on controlled protein packaging into plant PBs.

Indexed as

Biological ProductsGreen Fluorescent ProteinsRecombinant Fusion ProteinsZeinAdministration, OralCell LineHumansNicotianaPlant LeavesU937 CellsBiological ProductsGreen Fluorescent ProteinsRecombinant Fusion ProteinsZeinbioencapsulationmolecular farmingplant-made pharmaceuticalsprotein bodiesrecombinant proteins

Identifiers

PMID31956981
PMCPMC7079162
OpenAlexW3001429871

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.