Evidence map›Paper›PMID 24465364›Full record

ArticlePloS one2014

Canine parvovirus VP2 protein expressed in silkworm pupae self-assembles into virus-like particles with high immunogenicity.

Hao Feng, Gui-qiu Hu, Hua-lei Wang, Meng Liang, Hongru Liang, He Guo, Pingsen Zhao, Yu-jiao Yang, Xue-xing Zheng, Zhi-fang Zhang and 4 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
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  18. Edible Vaccines: Promises and Challenges.Molecular biotechnology · 2020
    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

14 authors at 5 institutions in 1 country.

Hao FengInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Gui-qiu HuAgricultural Division, College of Animal Science and Veterinary Medicine, Jilin University, Changchun, Jilin Province, China ; College of Animal Science and Technology, Jilin Agricultural University, Changchun, Jilin Province, China.
Hua-lei WangInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Meng LiangAgricultural Division, College of Animal Science and Veterinary Medicine, Jilin University, Changchun, Jilin Province, China.
Hongru LiangInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
He GuoAgricultural Division, College of Animal Science and Veterinary Medicine, Jilin University, Changchun, Jilin Province, China.
Pingsen ZhaoInstitute of Laboratory Animal Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College, Bejing, China.
Yu-jiao YangAgricultural Division, College of Animal Science and Veterinary Medicine, Jilin University, Changchun, Jilin Province, China.
Xue-xing ZhengInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Zhi-fang ZhangBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China.
Yong-kun ZhaoInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Yu-wei GaoInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Song-tao YangInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Xian-zhu XiaInstitute of Military Veterinary, Academy of Military Medical Sciences, Changchun, Jilin Province, China.
Academy of Military Medical Sciences · CNJilin Agricultural University · CNJilin University · CNBiotechnology Research Institute · CNChinese Academy of Medical Sciences & Peking Union Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The VP2 structural protein of parvovirus can produce virus-like particles (VLPs) by a self-assembly process in vitro, making VLPs attractive vaccine candidates. In this study, the VP2 protein of canine parvovirus (CPV) was expressed using a baculovirus expression system and assembled into parvovirus-like particles in insect cells and pupae. Electron micrographs of VLPs showed that they were very similar in size and morphology when compared to the wild-type parvovirus. The immunogenicity of the VLPs was investigated in mice and dogs. Mice immunized intramuscularly with purified VLPs, in the absence of an adjuvant, elicited CD4(+) and CD8(+) T cell responses and were able to elicit a neutralizing antibody response against CPV, while the oral administration of raw homogenates containing VLPs to the dogs resulted in a systemic immune response and long-lasting immunity. These results demonstrate that the CPV-VLPs stimulate both cellular and humoral immune responses, and so CPV-VLPs may be a promising candidate vaccine for the prevention of CPV-associated disease.

Indexed as

Virus AssemblyAnimalsAntibodiesBlotting, WesternBombyxCD4-Positive T-LymphocytesCD8-Positive T-LymphocytesCell ProliferationDog DiseasesDogsErythrocytesFluorescent Antibody TechniqueHemagglutinationHemagglutination Inhibition TestsImmunizationMiceAntibodiesViral ProteinsViral Vaccines

Identifiers

PMID24465364
PMCPMC3894932
OpenAlexW2084306029

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.