ArticleJournal of virology2026
Role of g5Rp in African swine fever virus replication: disruption of host translation and autophagy.
Article in Journal of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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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
2 citing papers in PubMed.
- ASFV MGF110-7L Inhibits eIF4G1 Expression via Endoplasmic Reticulum Stress to Block Host Translation.Viruses · 2026Article
- The implications of FASN in viral infection and related diseases: a promising target in antiviral therapies.Frontiers in cellular and infection microbiology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
Abstract
African swine fever (ASF), caused by the African swine fever virus (ASFV), is one of the most severe viral diseases affecting swine. ASFV employs sophisticated strategies to subvert host immune responses; however, the function of the viral protein g5Rp in viral pathogenesis remains incompletely defined. In this study, we demonstrate that g5Rp plays a critical role in viral replication by impairing host translation and autophagy. Overexpression of g5Rp enhanced viral replication and increased p30 protein levels, whereas siRNA-mediated knockdown of g5Rp suppressed both, underscoring its essential proviral function. Proteomic profiling of infected porcine macrophages (3D4/21 cells) revealed that g5Rp dysregulated 122 host proteins, predominantly involved in translation, autophagy, and apoptosis pathways. Mechanistically, g5Rp directly interacted with eIF5A and RPS15, disrupting their complex formation and thereby inhibiting translation initiation and autophagic flux. Structural analyses identified key residues (SER¹¹⁸, SER²⁰⁶, and ASN⁶¹) critical for this interference. Mutation of these residues abrogated g5Rp activity. Furthermore, virtual screening identified 9″-methyl salvianolate B as a potent g5Rp inhibitor, which restored eIF5A hypusination, promoted autophagy, and suppressed ASFV replication IMPORTANCE: ASFV has caused significant economic losses to the global pork industry, and no effective treatment or prevention currently exists. In this study, the interaction of g5Rp with the host proteins eIF5A and RPS15 was identified for the first time, and its crucial role in the viral life cycle was clarified. Resolving the crystal structure of g5Rp revealed its binding site to the host protein, which provides a new target for developing antiviral strategies against g5Rp. Additionally, the screened 9″-methyl salvianolate B, a small-molecule inhibitor, has shown the potential to effectively reduce viral replication and restore host protein synthesis. These findings not only deepen our understanding of the mechanism of ASFV infection but also lay the foundation for developing effective anti-ASFV treatment strategies in the future, which has important scientific implications.
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Registered trials
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.