Evidence map›Paper›PMID 19891790›Full record

ArticleVirology journal2009

Chimeric recombinant rotavirus-like particles as a vehicle for the display of heterologous epitopes.

Andrea Peralta, Paula Molinari, Oscar Taboga

Abstract read
In one paragraph

Article in Virology journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

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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.

Andrea PeraltaConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Av, Rivadavia 1917 (c,p,1033) Ciudad Autónoma de Buenos Aires, Argentina. avperalta@cnia.inta.gov.ar
Paula Molinari
Oscar Taboga

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to improve the presentation and immunogenicity of single epitopes, virus-like particles (VLPs) are being used as platforms for the display of foreing epitopes on their surface. The rotavirus major capsid protein VP6 has the ability to self-assemble into empty non-infectious VLPs. In the present study, we analyzed the use of double layered VLPs (made up of VP2 and VP6 rotavirus proteins) as carriers to display a 14 amino acid epitope fused to three different aminoacidic regions of VP6 exposed on the surface of VLPs. Although all chimeric protein were correctly expressed in insect cells, only one of them resulted in spontaneous assembly of VLPs displaying the heterologous epitope on their surface, confirmed by sandwich ELISA and electron microscopy. Furthermore, the injection of chimeric VLPs into mice elicited higher antibody titers than the monomeric chimeric protein. Our results identify an specific amino acid region of VP6 which allows the insertion of at least a 14 amino acid heterolgous epitope and demonstrate its potential as immunogenic carrier.

Indexed as

AnimalsAntibodies, ViralAntigens, ViralCapsid ProteinsCell LineEnzyme-Linked Immunosorbent AssayEpitopesFemaleMiceMice, Inbred BALB CMicroscopy, Electron, TransmissionMicroscopy, ImmunoelectronModels, MolecularProtein Structure, TertiaryRotavirusSpodopteraAntibodies, ViralAntigens, ViralCapsid ProteinsEpitopesVaccines, VirosomeViral VaccinesVirosomesVP2 protein, RotavirusVP6 protein, Rotavirus

Identifiers

PMID19891790
PMCPMC2777876

What OpenQuestion holds

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Registered trials

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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.