Evidence map›Paper›PMID 34228257›Full record

ArticleMolecular biotechnology2021

Production of Rabies VLPs in Insect Cells by Two Monocistronic Baculoviruses Approach.

Thaissa Consoni Bernardino, Renato Mancini Astray, Carlos Augusto Pereira, Vera Lucia Boldorini, Marta Maria Antoniazzi, Simone Gonçalves Silva Jared, Eutimio Gustavo Fernández Núñez, Soraia Attie Calil Jorge

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-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

12 citing papers in PubMed, 20 citations in OpenAlex.

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  10. The NPC Families Mediate BmNPV Entry.Microbiology spectrum · 2022
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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

8 authors at 2 institutions in 1 country.

Thaissa Consoni BernardinoLaboratório de Biotecnologia Viral, Instituto Butantan, Av Vital Brasil 1500, São Paulo, CEP, 05503-900, Brazil.
Renato Mancini AstrayLaboratório de Biotecnologia Viral, Instituto Butantan, Av Vital Brasil 1500, São Paulo, CEP, 05503-900, Brazil.
Carlos Augusto PereiraLaboratório de Biotecnologia Viral, Instituto Butantan, Av Vital Brasil 1500, São Paulo, CEP, 05503-900, Brazil.
Vera Lucia BoldoriniLaboratório de Biotecnologia Viral, Instituto Butantan, Av Vital Brasil 1500, São Paulo, CEP, 05503-900, Brazil.
Marta Maria AntoniazziLaboratório de Biologia Estrutural, Instituto Butantan, São Paulo-SP, Brazil.
Simone Gonçalves Silva JaredLaboratório de Biologia Estrutural, Instituto Butantan, São Paulo-SP, Brazil.
Eutimio Gustavo Fernández NúñezGrupo de Engenharia de Bioprocessos. Escola de Artes, Ciências E Humanidades (EACH), Universidade de São Paulo, São Paulo, SP, Brazil.
Soraia Attie Calil JorgeLaboratório de Biotecnologia Viral, Instituto Butantan, Av Vital Brasil 1500, São Paulo, CEP, 05503-900, Brazil. soraia.jorge@butantan.gov.br.ORCID http://orcid.org/0000-0001-9380-1023
Instituto Butantan · BRUniversidade de São Paulo · BR

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 152538/2012-7Fundação de Amparo à Pesquisa do Estado de São Paulo 2009/08038-1
6 · The paper itself

Abstract

Rabies is an ancient zoonotic disease that still causes the death of over 59,000 people worldwide each year. The rabies lyssavirus encodes five proteins, including the envelope glycoprotein and the matrix protein. RVGP is the only protein exposed on the surface of viral particle, and it can induce immune response with neutralizing antibody formation. RVM has the ability to assist with production process of virus-like particles. VLPs were produced in recombinant baculovirus system. In this work, two recombinant baculoviruses carrying the RVGP and RVM genes were constructed. From the infection and coinfection assays, we standardized the best multiplicity of infection and the best harvest time. Cell supernatants were collected, concentrated, and purified by sucrose gradient. Each step was used for protein detection through immunoassays. Sucrose gradient analysis enabled to verify the separation of VLPs from rBV. Through the negative contrast technique, we visualized structures resembling rabies VLPs produced in insect cells and rBV in the different fractions of the sucrose gradient. Using ELISA to measure total RVGP, the recovery efficiency of VLPs at each stage of the purification process was verified. Thus, these results encourage further studies to confirm whether rabies VLPs are a promising candidate for a veterinary rabies vaccine.

Indexed as

AnimalsBaculoviridaeCells, CulturedHumansInsectaRabiesRabies VaccinesRabies virusRecombinant ProteinsVaccines, Virus-Like ParticleRabies VaccinesRecombinant ProteinsVaccines, Virus-Like ParticleBaculovirusInsect cellsRabiesVirus-like Particles

Identifiers

PMID34228257
OpenAlexW3177558681

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.