Evidence map›Paper›PMID 30791210›Full record

ArticlePlant biotechnology journal2019

Immunogenicity of plant-produced porcine circovirus-like particles in mice.

Cornelius J Gunter, Guy L Regnard, Edward P Rybicki, Inga I Hitzeroth

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

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  9. A universal design of restructured dimer antigens: Development of a superior vaccine against the paramyxovirus in transgenic rice.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

4 authors at 1 institution in 1 country.

Cornelius J GunterBiopharming Research Unit, Department of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.
Guy L RegnardDivision of Medical Virology, Department of Pathology and Institute of Infectious Diseases and Molecular Medicine, Faculty of Health Sciences, University of Cape Town, Cape Town, South Africa.
Edward P RybickiBiopharming Research Unit, Department of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.ORCID 0000-0001-8024-9911
Inga I HitzerothBiopharming Research Unit, Department of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.ORCID 0000-0002-8515-9525
University of Cape Town · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Porcine circovirus type 2 (PCV-2) is the main causative agent associated with a group of diseases collectively known as porcine circovirus-associated disease (PCAD). There is a significant economic strain on the global swine industry due to PCAD and the production of commercial PCV-2 vaccines is expensive. Plant expression systems are increasingly regarded as a viable technology to produce recombinant proteins for use as pharmaceutical agents and vaccines. However, successful production and purification of PCV-2 capsid protein (CP) from plants is an essential first step towards the goal of a plant-produced PCV-2 vaccine candidate. In this study, the PCV-2 CP was transiently expressed in Nicotiana benthamiana plants via agroinfiltration and PCV-2 CP was successfully purified using sucrose gradient ultracentrifugation. The CP self-assembled into virus-like particles (VLPs) resembling native virions and up to 6.5 mg of VLPs could be purified from 1 kg of leaf wet weight. Mice immunized with the plant-produced PCV-2 VLPs elicited specific antibody responses to PCV-2 CP. This is the first report describing the expression of PCV-2 CP in plants, the confirmation of its assembly into VLPs and the demonstration of their use to elicit a strong immune response in a mammalian model.

Indexed as

CircovirusImmunogenicity, VaccineAnimalsAntibodies, ViralCapsid ProteinsMiceNicotianaPlants, Genetically ModifiedRecombinant ProteinsSwineVaccines, Virus-Like ParticleViral VaccinesAntibodies, ViralCapsid ProteinsRecombinant ProteinsVaccines, Virus-Like ParticleViral Vaccinesplant-producedporcine circovirus type 2purificationvaccinevirus-like particles

Identifiers

PMID30791210
PMCPMC6686138
OpenAlexW2916414460

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.