Evidence map›Paper›PMID 33559837›Full record

ArticleVirus genes2021

Mass spectrometry-based proteomic analysis of potential infectious bursal disease virus VP3-interacting proteins in chicken embryo fibroblasts cells.

Sun-Ting Ma, Yong-Shan Wang, Xiao-Li Wang, Xing-Xia Xia, Zhen-Wei Bi, Jing-Yu Wang, Yu-Mei Zhu, Wei Ouyang, Jing Qian

Abstract read
PubMed Publisher
In one paragraph

Article in Virus genes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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. The Formation and Function ofInternational journal of molecular sciences · 2023
    Review
  3. Ribosomal control in RNA virus-infected cells.Frontiers in microbiology · 2022
    Review
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

9 authors at 1 institution in 3 countries.

Sun-Ting MaInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Yong-Shan WangInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Xiao-Li WangInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Xing-Xia XiaInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Zhen-Wei BiInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Jing-Yu WangInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Yu-Mei ZhuInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Wei OuyangInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China. wei_ouyang2008@163.com.
Jing QianInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China. qjysb0110@126.com.ORCID http://orcid.org/0000-0001-8461-8999
Jiangsu Academy of Agricultural Sciences · CN

Funding

Jiangsu Agriculture Science and Technology Innovation Fund CX(19)3019Jiangsu Agriculture Science and Technology Innovation Fund CX(20)3095Jiangsu Provincial Natural Science Foundation of China BK20180299National Key R&D Program of China 2018YFD0500106National Natural Science Foundation of China 31772723National Natural Science Foundation of China 32002274National Natural Science Foundation of China 32072872
6 · The paper itself

Abstract

The structural protein VP3 of infectious bursal disease virus (IBDV) plays a critical role in viral assembly, replication, immune escape, and anti-apoptosis. Interaction between VP3 and host protein factors can affect stages in the viral replication cycle. In this study, 137 host proteins interacting with VP3 protein were screened through liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based proteomics approach. The functions and relevance of the proteins were obtained through bioinformatics analysis. Most VP3-interacting proteins were linked to binding, catalytic activity, and structural molecular activity, and performed functions in cell parts and cells. Biological functions of VP3-interacting proteins were mainly relevant to "Cytoskeleton", "Translation", and "Signal transduction mechanisms", involving ribosomes, "Tight junction", regulation of actin cytoskeleton, and other pathways. Six potential VP3-interacting proteins in host cells were knocked down, and vimentin, myosin-9, and annexin A2 were found to be related to IBDV replication. This study would help explore regulatory pathways and cellular mechanisms in IBDV-infected cells, and also provided clues for the in-depth study of VP3 biological functions and IBDV replication or pathogenesis.

Indexed as

AnimalsCell LineChick EmbryoChromatography, LiquidFibroblastsInfectious bursal disease virusProtein BindingProtein Interaction MapsProteinsProteomeTandem Mass SpectrometryViral Structural ProteinsVirus ReplicationProteinsProteomeViral Structural ProteinsVP3 protein, infectious bursal disease virusHost protein factorImmunoprecipitation techniqueInfectious bursal disease virusMass spectrometryVP3 protein

Identifiers

PMID33559837
OpenAlexW3126226231

What OpenQuestion holds

Textmetadata
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.