Evidence map›Paper›PMID 18540021›Full record

ArticleJournal of experimental botany2008

The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin.

Maddalena de Virgilio, Francesca De Marchis, Michele Bellucci, Davide Mainieri, Marika Rossi, Eugenio Benvenuto, Sergio Arcioni, Alessandro Vitale

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
9.4field-weighted citation impact, top 2% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Generation of multi-layered protein bodies inFrontiers in plant science · 2023
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Characterization and Immunogenicity of HIV Envelope gp140 ZeraFrontiers in bioengineering and biotechnology · 2020
    Article
  9. [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
  10. Article
  11. The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018
    Article
  12. Article
  13. Where do Protein Bodies of Cereal Seeds Come From?Frontiers in plant science · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

8 authors at 2 institutions in 1 country.

Maddalena de VirgilioIstituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, via Bassini 15, 20133 Milano, Italy, EU.
Francesca De Marchis
Michele Bellucci
Davide Mainieri
Marika Rossi
Eugenio Benvenuto
Sergio Arcioni
Alessandro Vitale
Istituto di Biologia e Biotecnologia Agraria · ITNational Agency for New Technologies, Energy and Sustainable Economic Development · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein bodies (PB) are stable polymers naturally formed by certain seed storage proteins within the endoplasmic reticulum (ER). The human immunodeficiency virus negative factor (Nef) protein, a potential antigen for the development of an anti-viral vaccine, is highly unstable when introduced into the plant secretory pathway, probably because of folding defects in the ER environment. The aim of this study was to promote the formation of Nef-containing PB in tobacco (Nicotiana tabacum) leaves by fusing the Nef sequence to the N-terminal domains of the maize storage protein gamma-zein or to the chimeric protein zeolin (which efficiently forms PB and is composed of the vacuolar storage protein phaseolin fused to the N-terminal domains of gamma-zein). Protein blots and pulse-chase indicate that fusions between Nef and the same gamma-zein domains present in zeolin are degraded by ER quality control. Consistently, a mutated zeolin, in which wild-type phaseolin was substituted with a defective version known to be degraded by ER quality control, is unstable in plant cells. Fusion of Nef to the entire zeolin sequence instead allows the formation of PB detectable by electron microscopy and subcellular fractionation, leading to zeolin-Nef accumulation higher than 1% of total soluble protein, consistently reproduced in independent transgenic plants. It is concluded that zeolin, but not its gamma-zein portion, has a positive dominant effect over ER quality control degradation. These results provide insights into the requirements for PB formation and avoidance of quality-control degradation, and indicate a strategy for enhancing foreign protein accumulation in plants.

Indexed as

Protein EngineeringAmino Acid SequenceAntigens, ViralGene ExpressionHumansInclusion BodiesMolecular Sequence Datanef Gene Products, Human Immunodeficiency VirusNicotianaPlant LeavesPlants, Genetically ModifiedProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsZea maysZeinAntigens, Viralnef Gene Products, Human Immunodeficiency Virusnef protein, Human immunodeficiency virus 1Recombinant Fusion ProteinsZeinEndoplasmic reticulumplant factoriesprotein accumulationprotein bodieszein

Identifiers

PMID18540021
PMCPMC2486477
OpenAlexW2111040866

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.