Evidence map›Paper›PMID 33806789›Full record

ArticleVaccines2021

Vaccine Efficacy of Self-Assembled Multimeric Protein Scaffold Particles Displaying the Glycoprotein Gn Head Domain of Rift Valley Fever Virus.

Paul J Wichgers Schreur, Mirriam Tacken, Benjamin Gutjahr, Markus Keller, Lucien van Keulen, Jet Kant, Sandra van de Water, Yanyin Lin, Martin Eiden, Melanie Rissmann and 7 more

Open access · goldAbstract read
In one paragraph

Article in Vaccines, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

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  17. Antimicrobial Potential of the GeneraAntibiotics (Basel, Switzerland) · 2022
    Review
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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

17 authors at 4 institutions in 3 countries.

Paul J Wichgers SchreurDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.ORCID 0000-0001-9790-2438
Mirriam TackenDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.
Benjamin GutjahrInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.
Markus KellerInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.ORCID 0000-0003-3229-8377
Lucien van KeulenDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.
Jet KantDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.
Sandra van de WaterDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.
Yanyin LinDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.
Martin EidenInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.ORCID 0000-0002-1197-8288
Melanie RissmannInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.
Felicitas von ArnimInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.
Rebecca KönigInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.
Alexander BrixBoehringer Ingelheim Veterinary Research Center GmbH & Co. KG, 30559 Hannover, Germany.
Catherine CharreyreBoehringer Ingelheim, 69007 Lyon, France.
Jean-Christophe AudonnetBoehringer Ingelheim, 69007 Lyon, France.
Martin H GroschupInstitute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.ORCID 0000-0003-0215-185X
Jeroen KortekaasDepartment of Virology, Wageningen Bioveterinary Research, 8221 RA Lelystad, The Netherlands.ORCID 0000-0002-0329-0176
Friedrich-Loeffler-Institut · DEWageningen University & Research · NLBoehringer Ingelheim (France) · FRBoehringer Ingelheim (Germany) · DE

Funding

Innovative Medicines Initiative 115760
6 · The paper itself

Abstract

Compared to free antigens, antigens immobilized on scaffolds, such as nanoparticles, generally show improved immunogenicity. Conventionally, antigens are conjugated to scaffolds through genetic fusion or chemical conjugation, which may result in impaired assembly or heterogeneous binding and orientation of the antigens. By combining two emerging technologies-i.e., self-assembling multimeric protein scaffold particles (MPSPs) and bacterial superglue-these shortcomings can be overcome and antigens can be bound on particles in their native conformation. In the present work, we assessed whether this technology could improve the immunogenicity of a candidate subunit vaccine against the zoonotic Rift Valley fever virus (RVFV). For this, the head domain of glycoprotein Gn, a known target of neutralizing antibodies, was coupled on various MPSPs to further assess immunogenicity and efficacy in vivo. The results showed that the Gn head domain, when bound to the lumazine synthase-based MPSP, reduced mortality in a lethal mouse model and protected lambs, the most susceptible RVFV target animals, from viremia and clinical signs after immunization. Furthermore, the same subunit coupled to two other MPSPs (

Indexed as

bacterial superglueGn head domainmultimeric protein scaffold particlesRift Valley fever virussheep

Identifiers

PMID33806789
PMCPMC8005036
OpenAlexW3137252893

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.