Evidence map›Paper›PMID 24914995›Full record

ArticlePloS one2014

Influence of elastin-like polypeptide and hydrophobin on recombinant hemagglutinin accumulations in transgenic tobacco plants.

Hoang Trong Phan, Bettina Hause, Gerd Hause, Elsa Arcalis, Eva Stoger, Daniel Maresch, Friedrich Altmann, Jussi Joensuu, Udo Conrad

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Transient Expression of Dengue Virus NS1 Antigen inFrontiers in plant science · 2019
    Article
  13. Article
  14. Article
  15. Frontiers in bioengineering and biotechnology · 2018
    Article
  16. Article
  17. Article
  18. Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.Journal of controlled release : official journal of the Controlled Release Society · 2016
    Review
  19. 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

9 authors at 6 institutions in 4 countries.

Hoang Trong PhanDepartment of Molecular Genetics, Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), Gatersleben, Germany; Department of Plant Cell Biotechnology, Institute of Biotechnology (IBT), Vietnam Academy of Science and Technology (VAST), Hanoi, Vietnam.
Bettina HauseCell and Metabolic Biology, Leibniz Institute of Plant Biochemistry (IPB), Halle, Germany.
Gerd HauseMicroscopy Unit, Biocenter, University of Halle-Wittenberg, Halle, Germany.
Elsa ArcalisMolecular Plant Physiology, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Eva StogerMolecular Plant Physiology, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Daniel MareschDepartment of Chemistry, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Friedrich AltmannDepartment of Chemistry, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Jussi JoensuuVTT Technical Research Centre of Finland, Espoo, Finland.
Udo ConradDepartment of Molecular Genetics, Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), Gatersleben, Germany.
BOKU University · ATLeibniz Institute of Plant Biochemistry · DELeibniz Institute of Plant Genetics and Crop Plant Research · DEMartin Luther University Halle-Wittenberg · DEVietnam Academy of Science and Technology · VNVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fusion protein strategies are useful tools to enhance expression and to support the development of purification technologies. The capacity of fusion protein strategies to enhance expression was explored in tobacco leaves and seeds. C-terminal fusion of elastin-like polypeptides (ELP) to influenza hemagglutinin under the control of either the constitutive CaMV 35S or the seed-specific USP promoter resulted in increased accumulation in both leaves and seeds compared to the unfused hemagglutinin. The addition of a hydrophobin to the C-terminal end of hemagglutinin did not significantly increase the expression level. We show here that, depending on the target protein, both hydrophobin fusion and ELPylation combined with endoplasmic reticulum (ER) targeting induced protein bodies in leaves as well as in seeds. The N-glycosylation pattern indicated that KDEL sequence-mediated retention of leaf-derived hemagglutinins and hemagglutinin-hydrophobin fusions were not completely retained in the ER. In contrast, hemagglutinin-ELP from leaves contained only the oligomannose form, suggesting complete ER retention. In seeds, ER retention seems to be nearly complete for all three constructs. An easy and scalable purification method for ELPylated proteins using membrane-based inverse transition cycling could be applied to both leaf- and seed-expressed hemagglutinins.

Indexed as

Blotting, WesternChromatography, AffinityElastinEndoplasmic ReticulumFluorescent Antibody TechniqueFungal ProteinsGlycosylationHemagglutininsInfluenza A Virus, H5N1 SubtypeMutagenesis, InsertionalNicotianaPeptidesPlant LeavesPlants, Genetically ModifiedRecombinant Fusion ProteinsSeedsElastinFungal ProteinsHemagglutininsPeptidesRecombinant Fusion Proteins

Identifiers

PMID24914995
PMCPMC4051685
OpenAlexW2024209235

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.