Evidence map›Paper›PMID 25045805›Full record

ArticleVaccine2014

Immunogenicity of recombinant VP2 proteins of all nine serotypes of African horse sickness virus.

Yuta Kanai, Piet A van Rijn, Mieke Maris-Veldhuis, Yuki Kaname, T N Athmaram, Polly Roy

Open access · hybridAbstract read
In one paragraph

Article in Vaccine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
10.9field-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

21 citing papers in PubMed, 34 citations in OpenAlex.

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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

6 authors at 4 institutions in 3 countries.

Yuta KanaiDepartment of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom.
Piet A van RijnDepartment of Virology, Central Veterinary Institute of Wageningen University (CVI), PO Box 65, 8200 AB Lelystad, The Netherlands; Department of Biochemistry, Centre for Human Metabonomics, North-West University, Private Bag X6001, Potchefstroom 2520, South Africa.
Mieke Maris-VeldhuisDepartment of Virology, Central Veterinary Institute of Wageningen University (CVI), PO Box 65, 8200 AB Lelystad, The Netherlands.
Yuki KanameDepartment of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom.
T N AthmaramDepartment of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom.
Polly RoyDepartment of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom. Electronic address: polly.roy@lshtm.ac.uk.
London School of Hygiene & Tropical Medicine · GBUniversity of London · GBNorth-West University · ZAWageningen University & Research · NL

Funding

Biotechnology and Biological Sciences Research Council BB/K015168/1
6 · The paper itself

Abstract

African horse sickness (AHS) is an equine disease with a mortality of up to 90% for susceptible horses. The causative agent AHS virus (AHSV) is transmitted by species of Culicoides. AHSV serogroup within the genus Orbivirus of the Reoviridae family consists of nine serotypes that show no or very limited cross-neutralization. Of the seven structural proteins (VP1-VP7) of AHSV, VP2 is the serotype specific protein, and the major target for neutralizing antibodies. In this report, recombinant VP2 proteins of all nine serotypes were expressed individually by the baculovirus expression system and the immunogenicity of each was studied by immunization of guinea pigs with single VP2 as well as with cocktails of VP2 proteins. Homologous neutralizing antibodies measured by 50% plaque reduction assay showed varying degrees (from 37 to 1365) of titers for different VP2 proteins. A low cross-neutralizing antibody titer was found for genetically related AHSV serotypes. Immunization with VP2 cocktails containing equal amounts of each of the VP2 proteins also triggered neutralizing antibodies albeit to lower titers (4-117) to each of the serotypes in the cocktail. This study is a first step to develop a VP2 subunit vaccine for AHS and our results indicate that VP2 subunit vaccines are feasible individually or in a multi-serotype cocktail.

Indexed as

African Horse SicknessAfrican Horse Sickness VirusAnimalsAntibodies, NeutralizingAntibodies, ViralBaculoviridaeCapsid ProteinsFemaleGuinea PigsNeutralization TestsRecombinant ProteinsSerogroupVaccines, SubunitViral VaccinesAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsRecombinant ProteinsVaccines, SubunitViral VaccinesVP2 protein, African horse sickness virusAfrican horse sicknessCapsid protein VP2Recombinant proteinSubunit vaccine

Identifiers

PMID25045805
PMCPMC4148702
OpenAlexW2018657005

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.