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Updated: Jan 9, 2026

Detection of Viral RNA by Fluorescence in situ Hybridization FISH
Published on: May 5, 2012
DDX21 nuclear-cytoplasmic shuttling recruits RPS18 to viral dsRNA to promote CSFV replication
Bingke Li1, Bolun Zhou2, Chenchen Sun1
1College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, China; Key Laboratory of Animal Vaccine Development, Ministry of Agriculture and Rural Affairs, Guangzhou 510642, China.
Classic Swine Fever Virus (CSFV) hijacks DEAD-box helicase 21 (DDX21), moving it to the cytoplasm. This interaction enhances viral protein synthesis by recruiting ribosomal protein S18 (RPS18), aiding CSFV replication.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- Cellular pathogens manipulate host cell machinery for replication.
- Nuclear protein relocalization is a key strategy employed by viruses.
Purpose of the Study:
- To elucidate the mechanism by which Classic Swine Fever Virus (CSFV) interacts with and hijacks host proteins.
- To investigate the role of DEAD-box helicase 21 (DDX21) in CSFV infection.
Main Methods:
- Investigated the dynamic translocation of DDX21 from the nucleus to the cytoplasm during CSFV infection.
- Analyzed the interaction between DDX21, ribosomal protein S18 (RPS18), and viral double-stranded RNA (dsRNA).
- Assessed the impact of the DDX21-RPS18 axis on viral protein synthesis.
Main Results:
- CSFV induces DDX21 translocation to the cytoplasm, where it acts as a scaffold for RPS18 binding to viral dsRNA.
- A feedback loop is established where DDX21 upregulates RPS18, and RPS18 suppresses DDX21 levels.
- RPS18 dose-dependently enhances viral NS4A protein synthesis, with DDX21's pro-viral activity being RPS18-dependent.
Conclusions:
- CSFV exploits DDX21 relocalization to hijack host translation machinery.
- The DDX21-RPS18 axis facilitates selective viral protein translation in the cytoplasm.
- Spatial control of RNA-binding proteins is a critical mechanism for pathogen replication.
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