Evidence map›Paper›PMID 28893289›Full record

ArticleVirology journal2017

Recombinant expression of beak and feather disease virus capsid protein and assembly of virus-like particles in Nicotiana benthamiana.

Guy L Regnard, Edward P Rybicki, Inga I Hitzeroth

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

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  10. Production of Biopharmaceuticals inFrontiers in plant science · 2019
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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

3 authors at 1 institution in 1 country.

Guy L RegnardBiopharming Research Unit, Department of Molecular and Cell Biology, Faculty of Science, University of Cape Town, Rondebosch 7701, Cape Town, South Africa.
Edward P RybickiBiopharming Research Unit, Department of Molecular and Cell Biology, Faculty of Science, University of Cape Town, Rondebosch 7701, Cape Town, South Africa.
Inga I HitzerothBiopharming Research Unit, Department of Molecular and Cell Biology, Faculty of Science, University of Cape Town, Rondebosch 7701, Cape Town, South Africa. inga.hitzeroth@uct.ac.za.
University of Cape Town · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBeak and feather disease virus (BFDV) is an important disease causing agent affecting psittacines. BFDV is highly infectious and can present as acute, chronic or subclinical disease. The virus causes immunodeficiency and is often associated with secondary infections. No commercial vaccine is available and yields of recombinant BFDV capsid protein (CP) expressed in insect cells and bacteria are yet to be seen as commercially viable, although both systems produced BFDV CP that could successfully assemble into virus-like particles (VLPs). Plants as expression systems are increasingly becoming favourable for the production of region-specific and niche market products. The aim of this study was to investigate the formation and potential for purification of BFDV VLPs in Nicotiana benthamiana.

methodsThe BFDV CP was transiently expressed in N. benthamiana using an Agrobacterium-mediated system and plant expression vectors that included a bean yellow dwarf virus (BeYDV)-based replicating DNA vector. Plant-produced BFDV CP was detected using immunoblotting. VLPs were purified using sucrose cushion and CsCl density gradient centrifugation and visualised using transmission electron microscopy.

resultsIn this study we demonstrate that the BFDV CP can be successfully expressed in N. benthamiana, albeit at relatively low yield. Using a purification strategy based on centrifugation we demonstrated that the expressed CP can self-assemble into VLPs that can be detected using electron microscopy. These plant-produced BFDV VLPs resemble those produced in established recombinant expression systems and infectious virions. It is possible that the VLPs are spontaneously incorporating amplicon DNA produced from the replicating BeYDV plant vector.

conclusionsThis is the first report of plant-made full-length BFDV CP assembling into VLPs. The putative pseudovirions could be used to further the efficacy of vaccines against BFDV.

Indexed as

Gene ExpressionNicotianaVirus AssemblyAnimalsCapsidCapsid ProteinsCentrifugation, Density GradientCircovirusGenetic VectorsMicroscopy, Electron, TransmissionPlants, Genetically ModifiedRecombinant ProteinsVaccines, Virus-Like ParticleCapsid ProteinsRecombinant ProteinsVaccines, Virus-Like ParticleBeak and feather disease virusCircovirusPlant-made pharmaceuticalSubunit vaccineVirus-like particle

Identifiers

PMID28893289
PMCPMC5594603
OpenAlexW2754206096

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.