ArticlemBio2026
The C-terminus of infectious bursal disease virus VP3 encodes a predicted intrinsically disordered region, which promotes the formation of cytoplasmic puncta and modulates their physical properties.
Article in mBio, 2026. 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
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Who cites it
1 citing paper in PubMed.
- Reassortment in infectious bursal disease virus (IBDV) and related birnaviruses.Journal of virology · 2026Review
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Authors and funding
6 authors.
Funding
Abstract
The virus factories (VFs) of infectious bursal disease virus (IBDV) are biomolecular condensates formed through liquid-liquid phase separation (LLPS). A major component of the IBDV VF is the nonstructural protein VP3, but the molecular basis underlying VF formation remains poorly understood. Here, we demonstrate that VP3 was necessary but not sufficient for phase-separated biomolecular condensates to form. Using live-cell imaging of cells transfected with fluorescent reporter-tagged proteins, our data suggested that the minimal components required to form these structures were VP3, the viral polymerase (VP1), and viral RNA (vRNA). Furthermore, using protein modeling and molecular dynamics simulations, we determined that the 36 amino acid carboxy (C)-terminus of VP3 forms a highly dynamic intrinsically disordered region (IDR). When this was removed, puncta were significantly less numerous ( IMPORTANCE: Liquid-liquid phase separation (LLPS) is a phenomenon of growing interest in cell biology. It is a part of the replication cycles of diverse viruses, but our understanding of the molecular basis that underpins the mechanism of phase separation is incomplete. We previously demonstrated that the virus factories of the birnavirus IBDV, a major agricultural pathogen, are biomolecular condensates formed through LLPS. In this study, we discovered that VP3 was necessary but not sufficient for condensates to form, and the minimal components of these structures were VP3, VP1, and likely vRNA. We also discovered that the C-terminal 36 amino acid region of IBDV VP3 encoded a highly dynamic intrinsically disordered region that promoted the formation of the cytoplasmic puncta and modulated their physical properties. This work contributes to a more detailed understanding of birnavirus replication at the molecular level and to the study of LLPS as a phenomenon.
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