Evidence map›Paper›PMID 29609659›Full record

ArticleVirology journal2018

Dengue virus-like particles mimic the antigenic properties of the infectious dengue virus envelope.

Stefan W Metz, Ashlie Thomas, Laura White, Mark Stoops, Markus Corten, Holger Hannemann, Aravinda M de Silva

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 66 citations in OpenAlex.

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  13. pr-independent biogenesis of infectious mature Zika virus particles.bioRxiv : the preprint server for biology · 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

7 authors at 1 institution in 1 country.

Stefan W MetzDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, USA. swmetz@med.unc.edu.ORCID 0000-0002-9249-2844
Ashlie ThomasDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, USA.
Laura WhiteDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, USA.
Mark StoopsDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, USA.
Markus CortenDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, USA.
Holger HannemannThe Native Antigen Company, Kidlington, Oxford, UK.
Aravinda M de SilvaDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, USA.
University of North Carolina at Chapel Hill · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
Protein Expression/Dengue Virology CoreU19AI109784 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TING, JENNY P · 2014 to 2018
$20.8M
NCI NIH HHS P30 CA016086NIAID NIH HHS U19 AI109784
6 · The paper itself

Abstract

backgroundThe 4 dengue serotypes (DENV) are mosquito-borne pathogens that are associated with severe hemorrhagic disease. DENV particles have a lipid bilayer envelope that anchors two membrane glycoproteins prM and E. Two E-protein monomers form head-to-tail homodimers and three E-dimers align to form "rafts" that cover the viral surface. Some human antibodies that strongly neutralize DENV bind to quaternary structure epitopes displayed on E protein dimers or higher order structures forming the infectious virus. Expression of prM and E in cell culture leads to the formation of DENV virus-like particles (VLPs) which are smaller than wildtype virus particles and replication defective due to the absence of a viral genome. There is no data available that describes the antigenic landscape on the surface of flavivirus VLPs in comparison to the better studied infectious virion.

methodsA large panel of well characterized antibodies that recognize epitope of ranging complexity were used in biochemical analytics to obtain a comparative antigenic surface view of VLPs in respect to virus particles. DENV patient serum depletions were performed the show the potential of VLPs in serological diagnostics.

resultsVLPs were confirmed to be heterogeneous in size morphology and maturation state. Yet, we show that many highly conformational and quaternary structure-dependent antibody epitopes found on virus particles are efficiently displayed on DENV1-4 VLP surfaces as well. Additionally, DENV VLPs can efficiently be used as antigens to deplete DENV patient sera from serotype specific antibody populations.

conclusionsThis study aids in further understanding epitopic landscape of DENV VLPs and presents a comparative antigenic surface view of VLPs in respect to virus particles. We propose the use VLPs as a safe and practical alternative to infectious virus as a vaccine and diagnostic antigen.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntigens, ViralCell LineChlorocebus aethiopsDengueDengue VaccinesDengue VirusEnzyme-Linked Immunosorbent AssayEpitopesHumansImmunoglobulin GNeutralization TestsVaccines, Virus-Like ParticleAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntigens, ViralDengue VaccinesEpitopesImmunoglobulin GVaccines, Virus-Like ParticleViral Envelope ProteinsDengue virusEpitopesSerum depletionsVLP

Identifiers

PMID29609659
PMCPMC5879749
OpenAlexW2800446413

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.