Evidence map›Paper›PMID 22424442›Full record

ArticleBMC plant biology2012

Proteomic characterisation of endoplasmic reticulum-derived protein bodies in tobacco leaves.

Minu Joseph, M Dolors Ludevid, Margarita Torrent, Valérie Rofidal, Marc Tauzin, Michel Rossignol, Jean-Benoit Peltier

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Characterization and Immunogenicity of HIV Envelope gp140 ZeraFrontiers in bioengineering and biotechnology · 2020
    Article
  9. Review
  10. [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
  11. Elevated COBMC plant biology · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

7 authors at 4 institutions in 3 countries.

Minu JosephCentre de Recerca en Agrigenòmica (CRAG)_CSIC-IRTA-UAB, Parc de Recerca UAB, Bellaterra (Cerdanyola del Vallés), 08193 Barcelona, Spain.
M Dolors Ludevid
Margarita Torrent
Valérie Rofidal
Marc Tauzin
Michel Rossignol
Jean-Benoit Peltier
Institut National de la Recherche Agronomique · MACenter for Research in Agricultural Genomics · ESCentre de Recerca en Sanitat Animal · ESSciences pour L’Œnologie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe N-terminal proline-rich domain (Zera) of the maize storage protein γ-zein, is able to induce the formation of endoplasmic reticulum (ER)-derived protein bodies (PBs) when fused to proteins of interest. This encapsulation enables a recombinant fused protein to escape from degradation and facilitates its recovery from plant biomass by gradient purification. The aim of the present work was to evaluate if induced PBs encapsulate additional proteins jointly with the recombinant protein. The exhaustive analysis of protein composition of PBs is expected to facilitate a better understanding of PB formation and the optimization of recombinant protein purification approaches from these organelles.

resultsWe analysed the proteome of PBs induced in Nicotiana benthamiana leaves by transient transformation with Zera fused to a fluorescent marker protein (DsRed). Intact PBs with their surrounding ER-membrane were isolated on iodixanol based density gradients and their integrity verified by confocal and electron microscopy. SDS-PAGE analysis of isolated PBs showed that Zera-DsRed accounted for around 85% of PB proteins in term of abundance. Differential extraction of PBs was performed for in-depth analysis of their proteome and structure. Besides Zera-DsRed, 195 additional proteins were identified including a broad range of proteins resident or trafficking through the ER and recruited within the Zera-DsRed polymer.

conclusionsThis study indicates that Zera-protein fusion is still the major protein component of the new formed organelle in tobacco leaves. The analysis also reveals the presence of an unexpected diversity of proteins in PBs derived from both the insoluble Zera-DsRed polymer formation, including ER-resident and secretory proteins, and a secretory stress response induced most likely by the recombinant protein overloading. Knowledge of PBs protein composition is likely to be useful to optimize downstream purification of recombinant proteins in molecular farming applications.

Indexed as

Endoplasmic ReticulumNicotianaPlant LeavesPlant ProteinsPlants, Genetically ModifiedProteomicsPlant Proteins

Identifiers

PMID22424442
PMCPMC3342223
OpenAlexW2059826143

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.