Evidence map›Paper›PMID 19234717›Full record

ArticlePlanta2009

High-level expression of the HIV-1 Pr55gag polyprotein in transgenic tobacco chloroplasts.

Nunzia Scotti, Fiammetta Alagna, Enrico Ferraiolo, Gelsomina Formisano, Lorenza Sannino, Luigi Buonaguro, Angelo De Stradis, Alessandro Vitale, Luigi Monti, Stefania Grillo and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
12.3field-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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 106 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Green Biologics: Harnessing the Power of Plants to Produce Pharmaceuticals.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Expression of LamB Vaccine Antigen inFrontiers in immunology · 2020
    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

12 authors at 5 institutions in 2 countries.

Nunzia ScottiCNR-IGV, Institute of Plant Genetics, National Research Council, Via Università 133, 80055 Portici, Italy. nscotti@unina.it
Fiammetta Alagna
Enrico Ferraiolo
Gelsomina Formisano
Lorenza Sannino
Luigi Buonaguro
Angelo De Stradis
Alessandro Vitale
Luigi Monti
Stefania Grillo
Franco M Buonaguro
Teodoro Cardi
National Research Council · ITNational Academies of Sciences, Engineering, and Medicine · USIstituto Nazionale Tumori IRCCS "Fondazione G. Pascale" · ITInstitute for Sustainable Plant Protection · ITIstituto di Biologia e Biotecnologia Agraria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants have been recognized as a promising production platform for recombinant pharmaceutical proteins. The human immunodeficiency virus Gag (Pr55(gag)) structural polyprotein precursor is a prime candidate for developing a HIV-1 vaccine, but, so far, has been expressed at very low level in plants. The aim of this study was to investigate factors potentially involved in Pr55(gag) expression and increase protein yield in plant cells. In transient expression experiments in various subcellular compartments, the native Pr55(gag) sequence could be expressed only in the chloroplast. Experiments with truncated subunits suggested a negative role of the 5'-end on the expression of the full gene in the cytosol. Stable transgenic plants were produced in tobacco by Agrobacterium-mediated nuclear transformation with protein targeted to plastids, and biolistic-mediated plastid transformation. Compared to the nuclear genome, the integration and expression of the gag transgene in the plastome resulted in significantly higher protein accumulation levels (up to 7-8% TSP, equivalent to 312-363 mg/kg FW). In transplastomic plants, a 25-fold higher protein accumulation was obtained by translationally fusing the Pr55(gag) polyprotein to the N-terminus of the plastid photosynthetic RbcL protein. In chloroplasts, the Pr55(gag) polyprotein was processed in a pattern similar to that achieved by the viral protease, the processing being more extended in older leaves of mature plants. The Gag proteins produced in transgenic plastids were able to assemble into particles resembling VLPs produced in baculovirus/insect cells and E. coli systems. These results indicate that plastid transformation is a promising tool for HIV antigen manufacturing in plant cells.

Indexed as

Chloroplastsgag Gene Products, Human Immunodeficiency VirusGene Expression Regulation, PlantGenetic VectorsHIV-1NicotianaPhenotypePlant LeavesPlants, Genetically ModifiedPolyproteinsRecombinant ProteinsTranscription, GeneticTransformation, GeneticTransgenesgag Gene Products, Human Immunodeficiency VirusPolyproteinsRecombinant Proteins

Identifiers

PMID19234717
OpenAlexW1997277765

What OpenQuestion holds

Textmetadata
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.