ArticleJournal of virology2026
SVCV phosphoprotein hijacks phase separation to immobilize the IRF3-TBK1 signaling axis and suppress interferon antiviral immunity.
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 1 paper.
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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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Who cites it
1 citing paper in PubMed.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spring viremia of carp virus (SVCV), a highly pathogenic rhabdovirus prevalent in fish, causes substantial mortality by evading host antiviral immunity; however, the underlying mechanisms remain incompletely understood. This study reveals a novel immune evasion strategy whereby the SVCV phosphoprotein (SVCV-P) hijacks the TBK1-IRF3 signaling axis via liquid-solid phase transition (LSPT), sequestering interferon regulatory factor 3 (IRF3) and inhibiting interferon (IFN) production. Upon stimulation, IRF3 facilitates TBK1 into functional liquid-liquid phase separation (LLPS) condensates, spatially enhancing IRF3 phosphorylation and downstream IFN responses. IRF3 acts as a scaffold via its DNA-binding domain (DBD) and intrinsically disordered region (IDR), while TBK1 incorporates via its kinase domain (KD), ubiquitin-like domain (ULD), and scaffold dimerization domain (SDD). Conversely, SVCV-P, driven by its IDRs and central domain (CD), undergoes robust LLPS, competitively recruiting TBK1 into SVCV-P-TBK1 condensates. These condensates merge with IRF3-TBK1 droplets, forming SVCV-P-TBK1-IRF3 ternary condensates. These subsequently undergo LSPT, immobilizing IRF3 and preventing its nuclear translocation.
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