Evidence map›Paper›PMID 38641833›Full record

ArticleVirology journal2024

Stability and integrity of self-assembled bovine parvovirus virus‑like particles (BPV‑VLPs) of VP2 and combination of VP1VP2 assisted by baculovirus-insect cell expression: a potential logistical platform for vaccine deployment.

Ashenafi Kiros Wubshet, Guo-Xiu Li, Qian Li, Jun-Fei Dai, Yao-Zhong Ding, Luoyi Zhou, Min Qu, Yang Wang, Zhongyuan Ma, Gebremeskel Mamu Werid and 6 more

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Production of recombinant goose parvovirus origin VP2 protein based on baculovirus expression system.Veterinary research forum : an international quarterly journal · 2026
    Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 3 countries.

Ashenafi Kiros WubshetState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Guo-Xiu LiState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Qian LiState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Jun-Fei DaiState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Yao-Zhong DingState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Luoyi ZhouState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Min QuState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Yang WangState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Zhongyuan MaState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Gebremeskel Mamu WeridDavies Livestock Research Centre, School of Animal & Veterinary Sciences, University of Adelaide, Roseworthy Campus, Roseworthy, SA, 5371, Australia.
Birhanu Hadush AberaDepartment of Veterinary Basics and Diagnostic Sciences, College of Veterinary Science, Mekelle University, 2084, Mekelle, Tigray, Ethiopia.
Asmelash Tassew KebedeState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Yuefeng SunState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Xiangping YinState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China.
Yongsheng LiuState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China. liuys4031@hevttc.edu.cn.
Zhang JieState Key Laboratory of Veterinary Etiological Biology, National/OIE Foot and Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, People's Republic of China. 4032@hevttc.edu.cn.
Lanzhou Veterinary Research Institute · CNChinese Academy of Agricultural Sciences · CNHunan University of Science and Technology · CNMekelle University · ETUniversity of Adelaide · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBovine parvovirus (BPV) is an autonomous DNA virus with a smaller molecular size and subtle differences in its structural proteins, unlike other animal parvoviruses. More importantly, this virus has the potential to produce visible to silent economic catastrophes in the livestock business, despite receiving very little attention. Parvoviral virus-like particles (VLPs) as vaccines and as logistical platforms for vaccine deployment are well studied. However, no single experimental report on the role of VP1 in the assembly and stability of BPV-VLPs is available. Furthermore, the self-assembly, integrity and stability of the VLPs of recombinant BPV VP2 in comparison to VP1 VP2 Cap proteins using any expression method has not been studied previously. In this study, we experimentally evaluated the self-assembling ability with which BPV virus-like particles (VLPs) could be synthesized from a single structural protein (VP2) and by integrating both VP2 and VP1 amino acid sequences.

methodsIn silico and experimental cloning methods were carried out. His-tagged and without-His-tag VP2 and V1VP2-encoding amino acid sequences were cloned and inserted into pFastbacdual, and insect cell-generated recombinant protein was evaluated by SDS‒PAGE and western blot. Period of infectivity and expression level were determined by IFA. The integrity and stability of the BPV VLPs were evaluated by transmission electron microscopy. The secondary structure of the BPV VLPs from both VP2 and V1VP2 was analyzed by circular dichroism.

resultsOur findings show that VP2 alone was equally expressed and purified into detectable proteins, and the stability at different temperatures and pH values was not appreciably different between the two kinds of VLPs. Furthermore, BPV-VP2 VLPs were praised for their greater purity and integrity than BPV-VP1VP2 VLPs, as indicated by SDS‒PAGE. Therefore, our research demonstrates that the function of VP1 has no bearing on the stability or integrity of BPV-VLPs.

conclusionsIn summary, incredible physiochemically stable BPV VP2-derived VLPs have been found to be promising candidates for the development of multivalent vaccines and immunodiagnostic kits against enteric viruses and to carry heterogeneous epitopes for various economically important livestock diseases.

Indexed as

BocavirusParvovirusVaccinesAnimalsBaculoviridaeCapsid ProteinsRecombinant ProteinsCapsid ProteinsRecombinant ProteinsVaccinesBovine parvovirusPhysicochemical propertiesSecondary structureVirus-like particleVP1VP2VP2

Identifiers

PMID38641833
PMCPMC11027344
OpenAlexW4394957204

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.