Evidence map›Paper›PMID 37046316›Full record

ArticleVirology journal2023

Screening and identification of cyprinid herpesvirus 2 (CyHV-2) ORF55-interacting proteins by phage display.

Min Qian, Simin Xiao, Yapeng Yang, Fei Yu, Jinxuan Wen, Liqun Lu, Hao Wang

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

Article in Virology journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 35% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Attenuation mechanisms of the P7-P8 live-attenuatedThe Journal of general virology · 2026
    Article
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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

7 authors at 2 institutions in 1 country.

Min QianNational Pathogen Collection Center for Aquatic Animals, Shanghai Ocean University, Shanghai, 201306, China.
Simin XiaoNational Pathogen Collection Center for Aquatic Animals, Shanghai Ocean University, Shanghai, 201306, China.
Yapeng YangNational Pathogen Collection Center for Aquatic Animals, Shanghai Ocean University, Shanghai, 201306, China.
Fei YuInstitute of Marine Biology, College of Oceanography, Hohai University, Nanjing, 210098, China.
Jinxuan WenNational Pathogen Collection Center for Aquatic Animals, Shanghai Ocean University, Shanghai, 201306, China.
Liqun LuNational Pathogen Collection Center for Aquatic Animals, Shanghai Ocean University, Shanghai, 201306, China.
Hao WangNational Pathogen Collection Center for Aquatic Animals, Shanghai Ocean University, Shanghai, 201306, China. h-wang@shou.edu.cn.
Shanghai Ocean University · CNHohai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCyprinid herpesvirus 2 (CyHV-2) is a pathogenic fish virus belonging to family Alloherpesviridae. The CyHV-2 gene encoding thymidine kinase (TK) is an important virulence-associated factor. Therefore, we aimed to investigate the biological function of open reading frame 55 (ORF55) in viral replication.

methodsPurified CyHV-2 ORF55 protein was obtained by prokaryotic expression, and the interacting peptide was screened out using phage display. Host interacting proteins were then predicted and validated.

resultsORF55 was efficiently expressed in the prokaryotic expression system. Protein and peptide interaction prediction and dot-blot overlay assay confirmed that peptides identified by phage display could interact with the ORF55 protein. Comparing the peptides to the National Center for Biotechnology Information database revealed four potential interacting proteins. Reverse transcription quantitative PCR results demonstrated high expression of an actin-binding Rho-activating protein in the latter stages of virus-infected cells, and molecular docking, cell transfection and coimmunoprecipitation experiments confirmed that it interacted with the ORF55 protein.

conclusionDuring viral infection, the ORF55 protein exerts its biological function through interactions with host proteins. The specific mechanisms remain to be further explored.

Indexed as

BacteriophagesCarpsFish DiseasesHerpesviridaeHerpesviridae InfectionsAnimalsMolecular Docking SimulationOpen Reading FramesCyprinid herpesvirus 2ORF55Phage display technologyProkaryotic expressionThymidine kinaseVirulence factor

Identifiers

PMID37046316
PMCPMC10091560
OpenAlexW4365148207

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.