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PreprintCited by 1Animal Virus Infections StudiesRNA Research and SplicingProtein Structure and Dynamics

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The C terminus of infectious bursal disease virus (IBDV) VP3 encodes a predicted intrinsically disordered region (IDR), which promotes the formation of cytoplasmic puncta and modulates their physical properties

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Brodrick, A.J., Broadbent, A. J.·2025·mBio
DOI 10.1101/2025.01.17.633518PMC PMC12893007

Preprint — published as 10.1128/mbio.03107-25

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Abstract

The virus factories (VFs) of infectious bursal disease virus (IBDV) form through liquid-liquid phase separation (LLPS). A major component of the IBDV VF is the nonstructural protein VP3. Here, we predicted the full-length structure of the VP3 monomer and homodimer and employed molecular dynamics simulations to characterize their behavior. We identified the 36 amino acid carboxy(C)-terminus as a highly dynamic intrinsically disordered region (IDR). We then compared the cytoplasmic puncta that were made in the presence of the wild type (wt) VP3 with those made with a VP3 that lacked the C-terminus (VP3ΔC). Using live-cell imaging with fluorescent reporter tagged proteins, we found that VP3ΔC puncta were significantly less numerous (p<0.0001), smaller (p<0.0001), and more irregular in shape than puncta formed in the presence of wt VP3, demonstrating that the VP3 C terminal IDR promoted their formation. Moreover, by fluorescence recovery after photobleaching (FRAP), the VP3ΔC puncta had a significantly reduced mobile fraction (0.29) as compared to full-length VP3 puncta (0.70) (p<0.001), demonstrating that the VP3 C terminal IDR modulated their physical properties. However, the VP3ΔC puncta still exhibited liquid-like fusion events in the cytoplasm and were sensitive to treatment with aliphatic diols. Moreover, VP3 did not form puncta when expressed alone, and the removal of the C terminus did not abolish puncta formation completely. We propose that VP3 forms part of a higher order complex with other biomolecules to drive LLPS, and that the VP3 C terminal IDR modulates the physical properties of the resultant LLPS structures. Importance: 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 birnavirus IBDV, a major agricultural pathogen, exploits LLPS in the formation of its VFs. Here, we have characterized the C-terminal 36 amino acid region of IBDV VP3 bioinformatically and by molecular dynamics simulations and found that it encodes a highly dynamic intrinsically disordered region (IDR). Furthermore, we found this region to promote the formation of cytoplasmic puncta and modulate 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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Figures

Fig 1 VP3 is necessary, but not sufficient, for the formation of IBDV cytoplasmic puncta. DF-1 cells were transfected with Segment A (SegA), HA::Segment B (HA::SegB), VP3 alone, or SegA + HA::SegB, SegAΔVP3 + HA::SegB, or SegAΔVP3 + HA::SegB + VP3 (A). Cells were fixed at 34 hpt and stained with DAPI (blue) and antibodies against VP3 (green) or HA (red). Mosaic images were acquired with the Leica Stellaris 8 scanning confocal microscope. Arrows denote puncta; scale bars, 50 µm.
Fig 1 VP3 is necessary, but not sufficient, for the formation of IBDV cytoplasmic puncta. DF-1 cells were transfected with Segment A (SegA), HA::Segment B (HA::SegB), VP3 alone, or SegA + HA::SegB, SegAΔVP3 + HA::SegB, or SegAΔVP3 + HA::SegB + VP3 (A). Cells were fixed at 34 hpt and stained with DAPI (blue) and antibodies against VP3 (green) or HA (red). Mosaic images were acquired with the Leica Stellaris 8 scanning confocal microscope. Arrows denote puncta; scale bars, 50 µm.CC BY · PubMed Central
Fig 2 Evaluating the expression of VP3 fused to different tags. DF-1 cells were transfected with a vector expressing VP3, or reporter-conjugated VP3 constructs (TC::VP3, eGFP::VP3, and mNG::VP3). Cells were imaged by confocal microscopy at 18 hpt, either alone (left column) or in cells simultaneously transfected with reporter::VP3 conjugates and infected with strain PBG98 IBDV (multiplicity of infection [MOI] = 5). Scale bars, 10 µm.
Fig 2 Evaluating the expression of VP3 fused to different tags. DF-1 cells were transfected with a vector expressing VP3, or reporter-conjugated VP3 constructs (TC::VP3, eGFP::VP3, and mNG::VP3). Cells were imaged by confocal microscopy at 18 hpt, either alone (left column) or in cells simultaneously transfected with reporter::VP3 conjugates and infected with strain PBG98 IBDV (multiplicity of infection [MOI] = 5). Scale bars, 10 µm.CC BY · PubMed Central
Fig 3 The minimal components of IBDV cytoplasmic puncta are VP3 and VP1. DF-1 cells were transfected with mNG::VP3, VP1::FLAG, VP3, HA::Segment B (HA::SegB) or a mixture of VP3 + HA::SegB (A). Cells were fixed at 34 hpt, and the nuclei were stained with DAPI (blue). mNG is shown in green, Segment B (visualized by staining with anti-HA monoclonal antibody) and VP1 (visualized by staining with anti-FLAG monoclonal antibody) are shown in red. Mosaic images were acquired with the Leica Stellaris 8 scanning confocal microscope. Scale bars, 50 µm.
Fig 3 The minimal components of IBDV cytoplasmic puncta are VP3 and VP1. DF-1 cells were transfected with mNG::VP3, VP1::FLAG, VP3, HA::Segment B (HA::SegB) or a mixture of VP3 + HA::SegB (A). Cells were fixed at 34 hpt, and the nuclei were stained with DAPI (blue). mNG is shown in green, Segment B (visualized by staining with anti-HA monoclonal antibody) and VP1 (visualized by staining with anti-FLAG monoclonal antibody) are shown in red. Mosaic images were acquired with the Leica Stellaris 8 scanning confocal microscope. Scale bars, 50 µm.CC BY · PubMed Central
Fig 4 The minimal components of IBDV phase-separated biomolecular condensates are VP3, VP1, and RNA. DF-1 cells were co-transfected with a mixture of mNG::VP3 and VP1::FLAG, and a time-lapse series was captured by live confocal microscopy at 34 hpt with a single iteration of point bleaching on the 5th frame (yellow arrowhead). Intensity data were extracted and used to calculate a FRAP recovery curve. Results are from three replicates; error bars = SEM (A). DF-1 cells were co-transfected with a mixture of mNG::VP3 and SegB, and a FRAP recovery curve was generated in the same way (B). Representative recovery images for a photobleached puncta formed in the presence of VP1::FLAG with the time post-bleach (t) shown in milliseconds (ms) (C). Representative recovery images for a photobleached puncta formed in the presence of SegB with the t post-bleach shown in s (D).
Fig 4 The minimal components of IBDV phase-separated biomolecular condensates are VP3, VP1, and RNA. DF-1 cells were co-transfected with a mixture of mNG::VP3 and VP1::FLAG, and a time-lapse series was captured by live confocal microscopy at 34 hpt with a single iteration of point bleaching on the 5th frame (yellow arrowhead). Intensity data were extracted and used to calculate a FRAP recovery curve. Results are from three replicates; error bars = SEM (A). DF-1 cells were co-transfected with a mixture of mNG::VP3 and SegB, and a FRAP recovery curve was generated in the same way (B). Representative recovery images for a photobleached puncta formed in the presence of VP1::FLAG with the time post-bleach (t) shown in milliseconds (ms) (C). Representative recovery images for a photobleached puncta formed in the presence of SegB with the t post-bleach shown in s (D).CC BY · PubMed Central
Fig 5 VP3 encodes a C-terminal domain with a predicted lack of secondary structure. A schematic of the IBDV genome architecture depicting Segment A encoding VP3 at the 3′ end of the coding strand, upstream of the 3′ non-coding region (NCR) and downstream of VP4 (A). A predicted structure for VP3, generated by AlphaFold2, visualized with UCSF ChimeraX, and colored by positional confidence (red indicates lower confidence; blue indicates higher confidence). The N-terminus, C-terminus, and hinge regions are labeled (B). A disorder plot of the VP3 from IBDV strain PBG98, with IUPred3 short disorder plotted on the y-axis against VP3 amino acid residue number on the x-axis. The horizontal dashed line represents an IUPred3 Short Disorder of 0.5 and the N-terminus, C-terminus, and hinge regions of VP3 are labeled (C).
Fig 5 VP3 encodes a C-terminal domain with a predicted lack of secondary structure. A schematic of the IBDV genome architecture depicting Segment A encoding VP3 at the 3′ end of the coding strand, upstream of the 3′ non-coding region (NCR) and downstream of VP4 (A). A predicted structure for VP3, generated by AlphaFold2, visualized with UCSF ChimeraX, and colored by positional confidence (red indicates lower confidence; blue indicates higher confidence). The N-terminus, C-terminus, and hinge regions are labeled (B). A disorder plot of the VP3 from IBDV strain PBG98, with IUPred3 short disorder plotted on the y-axis against VP3 amino acid residue number on the x-axis. The horizontal dashed line represents an IUPred3 Short Disorder of 0.5 and the N-terminus, C-terminus, and hinge regions of VP3 are labeled (C).CC BY · PubMed Central
Fig 6 The VP3 C-terminal domain is predicted to be a highly dynamic IDR. The mean relative B-factor, calculated from MD simulations of the VP3 monomer (6 independent 20 nanosecond simulations), was plotted on the y-axis against VP3 amino acid residue number on the x-axis. Error bars represent the standard error of the mean (SEM) (A). Pearson’s product moment correlation coefficient between the trajectories of each pair of atoms was calculated and plotted as a heatmap. Yellow represents perfect positive correlation, purple represents perfect negative correlation, and blue/teal suggests a lack of correlation (B). The movement of the atoms (average positional correlation coefficient) within the 36 amino acids of the C-terminus was compared to equally sized windows of 36 amino acids in length spanning the whole length of the VP3 protein sequence, and the P-values were plotted on the y-axis against the VP3 amino acid residue number on the x-axis. Regions of the VP3 region that were significantly more ordered than the C-terminus had a P value below the 0.05 cutoff (red line) (C).
Fig 6 The VP3 C-terminal domain is predicted to be a highly dynamic IDR. The mean relative B-factor, calculated from MD simulations of the VP3 monomer (6 independent 20 nanosecond simulations), was plotted on the y-axis against VP3 amino acid residue number on the x-axis. Error bars represent the standard error of the mean (SEM) (A). Pearson’s product moment correlation coefficient between the trajectories of each pair of atoms was calculated and plotted as a heatmap. Yellow represents perfect positive correlation, purple represents perfect negative correlation, and blue/teal suggests a lack of correlation (B). The movement of the atoms (average positional correlation coefficient) within the 36 amino acids of the C-terminus was compared to equally sized windows of 36 amino acids in length spanning the whole length of the VP3 protein sequence, and the P-values were plotted on the y-axis against the VP3 amino acid residue number on the x-axis. Regions of the VP3 region that were significantly more ordered than the C-terminus had a P value below the 0.05 cutoff (red line) (C).CC BY · PubMed Central
Fig 7 IBDV VP3 can exist as a homodimer with two C-terminal dynamic IDRs extending from the core. A cartoon rendering of the VP3 homodimer as predicted by AlphaFold3, visualized in UCSF ChimeraX, and colored by positional confidence (red indicates lower confidence; blue indicates higher confidence) (A). A solvent-accessible surface of the VP3 homodimer, visualized by UCSF ChimeraX, and colored by positional confidence (red indicates lower confidence; blue indicates higher confidence) (B). An ensemble of structures representing 10 evenly spaced timepoints of a single 20 nanosecond MD simulation. Structures were extracted from the trajectory and rendered as an ensemble in UCSF ChimeraX without alignment, colored by monomer (one monomer in purple, the other in pink) (C). The mean relative B-factor was calculated from the MD simulations of the VP3 homodimer (6 independent 20 nanosecond simulations) and plotted on the y-axis against the amino acid residue number of two VP3 monomers (A and B) concatenated on the x-axis. Error bars represent SEM (D).
Fig 7 IBDV VP3 can exist as a homodimer with two C-terminal dynamic IDRs extending from the core. A cartoon rendering of the VP3 homodimer as predicted by AlphaFold3, visualized in UCSF ChimeraX, and colored by positional confidence (red indicates lower confidence; blue indicates higher confidence) (A). A solvent-accessible surface of the VP3 homodimer, visualized by UCSF ChimeraX, and colored by positional confidence (red indicates lower confidence; blue indicates higher confidence) (B). An ensemble of structures representing 10 evenly spaced timepoints of a single 20 nanosecond MD simulation. Structures were extracted from the trajectory and rendered as an ensemble in UCSF ChimeraX without alignment, colored by monomer (one monomer in purple, the other in pink) (C). The mean relative B-factor was calculated from the MD simulations of the VP3 homodimer (6 independent 20 nanosecond simulations) and plotted on the y-axis against the amino acid residue number of two VP3 monomers (A and B) concatenated on the x-axis. Error bars represent SEM (D).CC BY · PubMed Central
Fig 8 The C-terminal IDR is not required for the recruitment of IBDV VP3 into VFs. AlphaFold3 predictions for the wt VP3 (magenta) and the VP3ΔC (cyan) were aligned with ChimeraX and overlaid (N terminal helices numbered H1–5) (A). DF-1 cells were transfected with mNG, mNG::VP3, mNG::VP3ΔC, or mNG::Cterm (B) or were co-transfected with the plasmids and simultaneously infected with IBDV strain PBG98 (MOI 5) (C). Cells were fixed at 12 hpi, and the nuclei were stained with DAPI (blue), and the mNG signal is shown in green. Scale bars, 10 µm.
Fig 8 The C-terminal IDR is not required for the recruitment of IBDV VP3 into VFs. AlphaFold3 predictions for the wt VP3 (magenta) and the VP3ΔC (cyan) were aligned with ChimeraX and overlaid (N terminal helices numbered H1–5) (A). DF-1 cells were transfected with mNG, mNG::VP3, mNG::VP3ΔC, or mNG::Cterm (B) or were co-transfected with the plasmids and simultaneously infected with IBDV strain PBG98 (MOI 5) (C). Cells were fixed at 12 hpi, and the nuclei were stained with DAPI (blue), and the mNG signal is shown in green. Scale bars, 10 µm.CC BY · PubMed Central
Fig 9 The IBDV VP3 C-terminal IDR is not required for the formation of cytoplasmic puncta. DF-1 cells were either transfected with SegA or HA::SegB and fixed and stained with anti-VP3 or anti-HA antibodies at 18 hpt, or DF-1 cells were simultaneously transfected with both SegA and SegB and fixed and stained with an anti-VP3 antibody at 18 hpt (A). DF-1 cells were either transfected with SegAΔC or HA::SegB, and were fixed and stained with anti-VP3 or anti-HA antibodies at 18 hpt, or DF-1 cells were simultaneously transfected with both SegAΔC and SegB, and fixed and stained with an anti-VP3 antibody at 18 hpt. The nuclei were stained with DAPI (blue), and the VP3 or HA-VP1 signals are shown in magenta. Scale bars, 10 µm (B).
Fig 9 The IBDV VP3 C-terminal IDR is not required for the formation of cytoplasmic puncta. DF-1 cells were either transfected with SegA or HA::SegB and fixed and stained with anti-VP3 or anti-HA antibodies at 18 hpt, or DF-1 cells were simultaneously transfected with both SegA and SegB and fixed and stained with an anti-VP3 antibody at 18 hpt (A). DF-1 cells were either transfected with SegAΔC or HA::SegB, and were fixed and stained with anti-VP3 or anti-HA antibodies at 18 hpt, or DF-1 cells were simultaneously transfected with both SegAΔC and SegB, and fixed and stained with an anti-VP3 antibody at 18 hpt. The nuclei were stained with DAPI (blue), and the VP3 or HA-VP1 signals are shown in magenta. Scale bars, 10 µm (B).CC BY · PubMed Central
Fig 10 The IBDV VP3 C-terminal IDR promotes the formation of cytoplasmic puncta and influences their size and morphology. DF-1 cells were co-transfected with either SegA and SegB::mNG or SegAΔC and SegB::mNG. From each of 3 replicates, 50 cells were randomly selected at 34 hpt, and their phenotype (punctate or non-punctate) was classified (A), and the puncta per cell were counted (B). Fifty cells prepared in the same manner were then imaged individually by confocal microscopy, and puncta were segmented by watershed segmentation and the area, perimeter, mean fluorescence intensity, intensity standard deviation, eccentricity, and geometric solidity (a measure of morphological “roundness” or “smoothness”) were measured with the Scikit-image python module (C–H).
Fig 10 The IBDV VP3 C-terminal IDR promotes the formation of cytoplasmic puncta and influences their size and morphology. DF-1 cells were co-transfected with either SegA and SegB::mNG or SegAΔC and SegB::mNG. From each of 3 replicates, 50 cells were randomly selected at 34 hpt, and their phenotype (punctate or non-punctate) was classified (A), and the puncta per cell were counted (B). Fifty cells prepared in the same manner were then imaged individually by confocal microscopy, and puncta were segmented by watershed segmentation and the area, perimeter, mean fluorescence intensity, intensity standard deviation, eccentricity, and geometric solidity (a measure of morphological “roundness” or “smoothness”) were measured with the Scikit-image python module (C–H).CC BY · PubMed Central
Fig 11 The VP3 C-terminal IDR significantly contributes to the mobile fraction of the molecules within the cytoplasmic puncta. DF-1 cells were co-transfected with a mixture of SegA and SegB::mNG, and a time-lapse series was captured by live confocal microscopy at 14 hpt with a single iteration of point bleaching on the 5th frame (yellow arrowhead). Intensity data were extracted and used to calculate a FRAP recovery curve. Results are from three replicates; error bars = SEM (A). DF-1 cells were co-transfected with a mixture of SegAΔC and SegB::mNG, and a FRAP recovery curve was generated in the same way (B). Representative recovery images for a photobleached puncta formed in the presence of SegA with the time post-bleach (t) shown in milliseconds (ms) (C). Representative recovery images for a photobleached puncta formed in the presence of SegAΔC with the t post-bleach shown in ms (D).
Fig 11 The VP3 C-terminal IDR significantly contributes to the mobile fraction of the molecules within the cytoplasmic puncta. DF-1 cells were co-transfected with a mixture of SegA and SegB::mNG, and a time-lapse series was captured by live confocal microscopy at 14 hpt with a single iteration of point bleaching on the 5th frame (yellow arrowhead). Intensity data were extracted and used to calculate a FRAP recovery curve. Results are from three replicates; error bars = SEM (A). DF-1 cells were co-transfected with a mixture of SegAΔC and SegB::mNG, and a FRAP recovery curve was generated in the same way (B). Representative recovery images for a photobleached puncta formed in the presence of SegA with the time post-bleach (t) shown in milliseconds (ms) (C). Representative recovery images for a photobleached puncta formed in the presence of SegAΔC with the t post-bleach shown in ms (D).CC BY · PubMed Central
Fig 12 Puncta formed in the presence or absence of the VP3 C-terminal IDR are dynamic. DF-1 cells were transfected with a mixture of SegA and SegB::mNG (A), or DF-1 cells were transfected with a mixture of SegAΔC and SegB::mNG (B). At 34 hpt, cells were imaged by live-cell confocal microscopy, capturing images every five frames to make a time lapse. Still frames from the timelapses are shown. The leftmost images show whole-cell images (mNG signal shown in white), with stills from the inset regions (orange boxed regions) shown thereafter. The timestamp (t) of imaging is shown in seconds (s). Arrows show individual puncta that undergo fusion.
Fig 12 Puncta formed in the presence or absence of the VP3 C-terminal IDR are dynamic. DF-1 cells were transfected with a mixture of SegA and SegB::mNG (A), or DF-1 cells were transfected with a mixture of SegAΔC and SegB::mNG (B). At 34 hpt, cells were imaged by live-cell confocal microscopy, capturing images every five frames to make a time lapse. Still frames from the timelapses are shown. The leftmost images show whole-cell images (mNG signal shown in white), with stills from the inset regions (orange boxed regions) shown thereafter. The timestamp (t) of imaging is shown in seconds (s). Arrows show individual puncta that undergo fusion.CC BY · PubMed Central
Fig 13 Puncta formed in the presence or absence of the VP3 C-terminal IDR are sensitive to aliphatic diol treatment. DF-1 cells were transfected with a mixture of SegA and SegB::mNG (A), or DF-1 cells were transfected with a mixture of SegAΔC and SegB::mNG (B). Transfected cells were treated with 1,3-Propanediol (1,3-PD) while capturing time-lapse images. Briefly, cells were initially maintained in media for acquisition, and at time (t) = 0 seconds (s), 1,3-PD was added to achieve a final concentration of 4% (vol/vol). The leftmost images show whole cells (mNG signal shown in white), with stills from the inset regions (orange boxed regions) shown thereafter. The timestamp (t) of imaging is shown in seconds (s).
Fig 13 Puncta formed in the presence or absence of the VP3 C-terminal IDR are sensitive to aliphatic diol treatment. DF-1 cells were transfected with a mixture of SegA and SegB::mNG (A), or DF-1 cells were transfected with a mixture of SegAΔC and SegB::mNG (B). Transfected cells were treated with 1,3-Propanediol (1,3-PD) while capturing time-lapse images. Briefly, cells were initially maintained in media for acquisition, and at time (t) = 0 seconds (s), 1,3-PD was added to achieve a final concentration of 4% (vol/vol). The leftmost images show whole cells (mNG signal shown in white), with stills from the inset regions (orange boxed regions) shown thereafter. The timestamp (t) of imaging is shown in seconds (s).CC BY · PubMed Central
Fig 14 Schematic of the model for how VP1, VP3, and vRNA interact in a phase-separated biomolecular condensate. VP3 (blue) interacts with RNA (green) via the core domain, and with VP1 (magenta) via the C-terminus. Interaction of VP3 with VP1 increases the synthesis of dsRNA by the polymerase, which contributes to the growing condensate.
Fig 14 Schematic of the model for how VP1, VP3, and vRNA interact in a phase-separated biomolecular condensate. VP3 (blue) interacts with RNA (green) via the core domain, and with VP1 (magenta) via the C-terminus. Interaction of VP3 with VP1 increases the synthesis of dsRNA by the polymerase, which contributes to the growing condensate.CC BY · PubMed Central

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Metadata

Authors
Brodrick, A. J., & Broadbent, A. J.
Affiliations
University of Maryland, College Park (US)
Corresponding author
Broadbent, A. J.
ORCID
Venue
mBio
Publisher
openRxiv
Published
2025-01-18
Volume
17
Issue
2
Pages
e0310725-e0310725
ISSN
2150-7511 (ISSN-L)
DOI
10.1101/2025.01.17.633518
PMC
PMC12893007
OpenAlex
W7122837825
Cited by
1
References
1
Citations by year
2026: 1
FWCI
3.87
Type
journal article
Language
en
Open access
Licence
Locations
  • mBio (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institutes of Health (1s10od034260-01, 1s10od025223-01a1)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
infectious bursal disease virus, VP3, intrinsically disordered regions, liquid-liquid phase separation, biomolecular condensates, virus factories, VP1, viral RNA, viral replication, birnavirus, molecular dynamics simulation, FRAP, live-cell imaging, protein-protein interaction
MeSH terms
Biomolecular Condensates, Phase Separation, Animals, Cell Line, Cytoplasm, Infectious bursal disease virus, RNA, Viral, Virus Replication, Viral Structural Proteins, Viral Nonstructural Proteins, Molecular Dynamics Simulation, Intrinsically Disordered Proteins

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CoChat. (2026). Citation check: The C terminus of infectious bursal disease virus (IBDV) VP3 encodes a predicted intrinsically disordered region (IDR), which promotes the formation of cytoplasmic puncta and modulates their physical properties. https://app.cochat.ai/papers/10.1101/2025.01.17.633518
The paper
Brodrick, A. J., & Broadbent, A. J. (2025). The C terminus of infectious bursal disease virus (IBDV) VP3 encodes a predicted intrinsically disordered region (IDR), which promotes the formation of cytoplasmic puncta and modulates their physical properties. mBio. https://doi.org/10.1101/2025.01.17.633518

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.