Evidence map›Paper›PMID 29921294›Full record

ArticleVirology journal2018

Trigger factor assisted self-assembly of canine parvovirus VP2 protein into virus-like particles in Escherichia coli with high immunogenicity.

Liangliang Nan, Yunchao Liu, Pengchao Ji, Hua Feng, Chen Chen, Juan Wang, Dongmin Liu, Yinglei Cui, Yanwei Wang, Yafei Li and 2 more

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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 16% 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

6 citing papers in PubMed, 14 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

12 authors at 5 institutions in 1 country.

Liangliang NanCollege of Veterinary Medicine, Northwest A&F University, Yangling, 712100, China.
Yunchao LiuHenan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, 450002, China.
Pengchao JiCollege of Animal Science and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002, China.
Hua FengHenan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, 450002, China.
Chen ChenCollege of Veterinary Medicine, Northwest A&F University, Yangling, 712100, China.
Juan WangHenan Zhongze Biological Engineering Co., Ltd., Zhengzhou, 450019, China.
Dongmin LiuHenan Zhongze Biological Engineering Co., Ltd., Zhengzhou, 450019, China.
Yinglei CuiHenan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, 450002, China.
Yanwei WangHenan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, 450002, China.
Yafei LiCollege of Veterinary Medicine, Northwest A&F University, Yangling, 712100, China.
Enmin ZhouCollege of Veterinary Medicine, Northwest A&F University, Yangling, 712100, China.
Gaiping ZhangCollege of Veterinary Medicine, Northwest A&F University, Yangling, 712100, China. zhanggaiping2003@163.com.ORCID 0000-0002-9977-5599
Henan Academy of Agricultural Sciences · CNHenan Science and Technology Department · CNNorthwest A&F University · CNHenan Agricultural University · CNNorth West Agriculture and Forestry University · CN

Funding

National Key Research and Development Program of China 2016YFD0500704
6 · The paper itself

Abstract

Canine parvovirus (CPV) has been considered to be an important pathogen, which can cause acute infectious disease in canids. Although current vaccines are effective in preventing CPV infection, safety problems still remain unsolved. In this study, a subunit vaccine against CPV based on virus-like particles (VLPs) with good safety and immunogenicity is reported. Soluble CPV VP2 protein was produced by co-expression of chaperone trigger factor (Tf16) in Escherichia coli (E.coli), and assembled into CPV VLPs which could be affected by NaCl and pH. At 250 mM NaCl pH 8.0, the VLPs co-expressed with Tf16 had similar size (25 nm) and shape with the authentic virus capsid under the transmission electron microscopy (TEM), which is also in accordance with the dynamic light scattering (DLS) data. Immunization with these particles could induce high-titer hemagglutination inhibition (1:12288) and neutralizing antibodies (1:6144) in guinea pigs. Splenic cells of them could secrete IFN-γ and IL-4 after stimulation by CPV. Thus, the VLPs produced by the new approach with high yield and immunogenicity could be a potential candidate for CPV vaccine.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsCatsCell LineCytokinesDogsEscherichia coliFemaleGuinea PigsHemagglutination Inhibition TestsNeutralization TestsParvoviridae InfectionsParvovirus, CanineVaccines, SubunitAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsCytokinesVaccines, SubunitVaccines, Virus-Like ParticleCanine parvovirusEscherichia coliImmunogenicityTrigger factor 16Virus-like particle

Identifiers

PMID29921294
PMCPMC6008937
OpenAlexW2809381654

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.