Evidence map›Paper›PMID 32244384›Full record

ArticleViruses2020

A Heterologous Viral Protein Scaffold for Chimeric Antigen Design: An Example PCV2 Virus Vaccine Candidate.

Emilio Lamazares, Fernando Gutiérrez, Angela Hidalgo, Nicolas A Gutiérrez, Felipe I Espinoza, Oliberto Sánchez, Marcelo Cortez-San Martín, Carolina Mascayano, Javier González, José Saavedra and 4 more

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 98% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

14 authors at 5 institutions in 3 countries.

Emilio LamazaresBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.ORCID 0000-0002-2955-6534
Fernando GutiérrezBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.
Angela HidalgoBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.ORCID 0000-0003-0600-5243
Nicolas A GutiérrezBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.
Felipe I EspinozaBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.
Oliberto SánchezBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.
Marcelo Cortez-San MartínMolecular Virology and Pathogen Control Laboratory, Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Alameda 3363, Correo 40, Casilla 33, Santiago 9170022, Chile.
Carolina MascayanoDepartamento de Ciencias del Ambiente, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Alameda 3363, Correo 40, Casilla 33, Santiago 9170022, Chile.
Javier GonzálezNatural History Museum of Potsdam, 14467 Potsdam, Germany.
José SaavedraMolecular Virology and Pathogen Control Laboratory, Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Alameda 3363, Correo 40, Casilla 33, Santiago 9170022, Chile.
Claudia AltamiranoLaboratorio of Cultivos Celulares, Escuela de Ingeniería Bioquímica, Pontificia Universidad Católica de Valparaíso, Ave. Brasil 2085, Valparaíso 2362803, Chile.ORCID 0000-0002-6389-086X
Manuel MansurModerna Therapeutics 100 Upland Rd., Norwood, MA 02062, USA.
Álvaro RuizPathology and Preventive Medicine Department, School of Veterinary Sciences, Universidad de Concepción, Ave. Vicente Méndez 595, Chillan 3812120, Chile.ORCID 0000-0002-3606-0860
Jorge R ToledoBiotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile.
University of Concepción · CLUniversidad de Santiago de Chile · CLDeutsche Meeresmuseum · DEModerna Therapeutics (United States) · USPontificia Universidad Católica de Valparaíso · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant vaccines have low-cost manufacturing, regulatory requirements, and reduced side effects compared to attenuated or inactivated vaccines. In the porcine industry, post-weaning multisystemic disease syndrome generates economic losses, characterized by progressive weight loss and weakness in piglets, and it is caused by porcine circovirus type 2 (PCV2). We designed a chimeric antigen (Qm1) to assemble the main exposed epitopes of the Cap-PCV2 protein on the capsid protein of the tobacco necrosis virus (TNV). This design was based on the Cap-N-terminal of an isolated PCV2 virus obtained in Chile. The virus was characterized, and the sequence was clustered within the PCV2 genotype b clade. This chimeric protein was expressed as inclusion bodies in both monomeric and multimeric forms, suggesting a high-molecular-weight aggregate formation. Pigs immunized with Qm1 elicited a strong and specific antibody response, which reduced the viral loads after the PCV2 challenge. In conclusion, the implemented design allowed for the generation of an effective vaccine candidate. Our proposal could be used to express the domains or fragments of antigenic proteins, whose structural complexity does not allow for low-cost production in

Indexed as

AnimalsAntibodies, ViralAntigens, ViralCapsid ProteinsChileCircoviridae InfectionsCircovirusEpitopesFermentationPhylogenyPorcine Postweaning Multisystemic Wasting SyndromeSwineTombusviridaeVaccinationVaccines, SyntheticViral VaccinesAntibodies, ViralAntigens, ViralCapsid ProteinsEpitopesVaccines, SyntheticViral Vaccinesbiotechnology strategiesPCV2 virusrecombinant antigens productionvaccines

Identifiers

PMID32244384
PMCPMC7232224
OpenAlexW3014841109

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.