Evidence map›Paper›PMID 19175916›Full record

ArticleBMC biology2009

Eukaryotic protein production in designed storage organelles.

Margarita Torrent, Blanca Llompart, Sabine Lasserre-Ramassamy, Immaculada Llop-Tous, Miriam Bastida, Pau Marzabal, Ann Westerholm-Parvinen, Markku Saloheimo, Peter B Heifetz, M Dolors Ludevid

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
13.5field-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

58 citing papers in PubMed, 141 citations in OpenAlex.

  1. Vaccines · 2025
    Article
  2. Article
  3. Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023
    Review
  4. Generation of multi-layered protein bodies inFrontiers in plant science · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Characterization and Immunogenicity of HIV Envelope gp140 ZeraFrontiers in bioengineering and biotechnology · 2020
    Article
  19. [Transient expression of bioactive recombinant human plasminogen activator in tobacco leaf].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2019
    Article
  20. Article
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

10 authors at 3 institutions in 2 countries.

Margarita TorrentDepartament de Genètica Molecular, Consorci CSIC-IRTA, Jordi Girona, Barcelona, Spain. mtqgmd@cid.csic.es
Blanca Llompart
Sabine Lasserre-Ramassamy
Immaculada Llop-Tous
Miriam Bastida
Pau Marzabal
Ann Westerholm-Parvinen
Markku Saloheimo
Peter B Heifetz
M Dolors Ludevid
SOM Biotech (Spain) · ESVTT Technical Research Centre of Finland · FIConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein bodies (PBs) are natural endoplasmic reticulum (ER) or vacuole plant-derived organelles that stably accumulate large amounts of storage proteins in seeds. The proline-rich N-terminal domain derived from the maize storage protein gamma zein (Zera) is sufficient to induce PBs in non-seed tissues of Arabidopsis and tobacco. This Zera property opens up new routes for high-level accumulation of recombinant proteins by fusion of Zera with proteins of interest. In this work we extend the advantageous properties of plant seed PBs to recombinant protein production in useful non-plant eukaryotic hosts including cultured fungal, mammalian and insect cells.

resultsVarious Zera fusions with fluorescent and therapeutic proteins accumulate in induced PB-like organelles in all eukaryotic systems tested: tobacco leaves, Trichoderma reesei, several mammalian cultured cells and Sf9 insect cells. This accumulation in membranous organelles insulates both recombinant protein and host from undesirable activities of either. Recombinant protein encapsulation in these PBs facilitates stable accumulation of proteins in a protected sub-cellular compartment which results in an enhancement of protein production without affecting the viability and development of stably transformed hosts. The induced PBs also retain the high-density properties of native seed PBs which facilitate the recovery and purification of the recombinant proteins they contain.

conclusionThe Zera sequence provides an efficient and universal means to produce recombinant proteins by accumulation in ER-derived organelles. The remarkable cross-kingdom conservation of PB formation and their biophysical properties should have broad application in the manufacture of non-secreted recombinant proteins and suggests the existence of universal ER pathways for protein insulation.

Indexed as

AnimalsBiotechnologyCell LineCHO CellsCricetinaeCricetulusEukaryotic CellsGene Expression RegulationNicotianaOrganellesPlant ProteinsRecombinant ProteinsTrichodermaZea maysZeinPlant ProteinsRecombinant ProteinsZein

Identifiers

PMID19175916
PMCPMC2637842
OpenAlexW1975513263

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.