ArticleVeterinary research2025
DTMUV upregulates DDX17 expression to facilitate viral replication.
Article in Veterinary research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
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.
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Who cites it
1 citing paper in PubMed.
- The scorpion peptide Eval418 inhibits duck Tembusu virus replication by disrupting viral structure and early-stage infection.Frontiers in veterinary science · 2026Article
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Authors and funding
12 authors.
Funding
Abstract
Duck Tembusu virus (DTMUV) is a single-stranded positive-sense RNA virus that poses a serious threat to the poultry industry, and its infection mechanism remains incompletely understood. This study aimed to investigate the role of the host protein DDX17 (DEAD-box RNA helicase 17) in DTMUV infection. Utilizing an in vitro infection model combined with CRISPR/Cas9 gene knockout, siRNA interference, and overexpression techniques, we found that DTMUV infection significantly upregulated both mRNA and protein expression levels of DDX17 in host cells. Furthermore, DDX17 facilitated viral replication through its ATP-binding and hydrolysis domain. Co-immunoprecipitation and mass spectrometry analysis confirmed an interaction between DDX17 and the DTMUV C protein. Additionally, phylogenetic analysis revealed that duck DDX17 shares the highest homology (99.8%) with avian orthologs, and tissue distribution assays indicated its highest expression levels in the spleen and liver. This study is the first to reveal the replication-promoting role of DDX17 in avian DTMUV infection and further elucidates its molecular mechanism involving interaction with the viral C protein, providing a theoretical basis for antiviral strategies targeting host factors.
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Registered trials
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