{
  "abstract": "BackgroundNewcastle disease virus (NDV) infects more than 250 avian species and mammals. Cytoplasmic inclusion bodies (IBs) are a hallmark of paramyxovirus infection; however, the molecular mechanisms underlying NDV IB formation remain poorly understood.MethodsIn this study, we investigated the interactive sites of viral protein driving IB-like structure formation via transmission electron microscopy, immunofluorescence assays (IFA), viral titration, co-immunoprecipitation (co-IP), structural modeling analysis.ResultsBoth virulent and attenuated NDV strains induced IBs in chicken-, mouse-, and human-derived cells. And the virus replicated well in CEF and HeLa cells rather than MEF. Time-course analysis revealed that IBs emerged as small puncta early in infection, increased in size over time, and ultimately accumulated in the perinuclear region. Co-immunoprecipitation (co-IP) and IFA revealed that amino acid residues 367–375 of the nucleoprotein (NP) bound to the PMD of the phosphoprotein (P), and this interaction was required for IB-like structure assembly. Furthermore, structural modeling and experiments of the NP–P complex identified residues Gln370 of NP and residue Ser254 of P as the principal contact and interacting sites for IB-like structure assembly.DiscussionThese findings reveal a previously unrecognized NP–P binding interface that mediates NDV IB formation, providing new insights into the molecular basis of viral condensate biogenesis in paramyxoviruses and a potential target for antiviral intervention.",
  "abstract_shown": true,
  "affiliations": [
    "Poultry Institute, Shandong Academy of Agricultural Science, Jinan, China",
    "Jinan Key Laboratory for Agricultural Experimental Animal and Comparative Medicine, Jinan, China",
    "Shandong Provincial Key Laboratory of Livestock and Poultry Breeding (PKL2024B15), Shandong Academy of Agricultural Sciences, Jinan, China",
    "College of Veterinary Medicine, Northwest A&F University, Yangling, China",
    "Institute of Experimental Veterinary Medicine named of S.N. Vyshelessky, Minsk, Belarus"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 29,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Wenbin Wang"
    },
    {
      "affs": [
        1
      ],
      "name": "Wenbin Wang"
    },
    {
      "affs": [
        2
      ],
      "name": "Wenbin Wang"
    },
    {
      "affs": [
        3
      ],
      "name": "Sa Xiao"
    },
    {
      "affs": [
        0
      ],
      "name": "Yuxia Zhang"
    },
    {
      "affs": [
        1
      ],
      "name": "Yuxia Zhang"
    },
    {
      "affs": [
        2
      ],
      "name": "Yuxia Zhang"
    },
    {
      "affs": [
        0
      ],
      "name": "Xiaoyuan Yuan"
    },
    {
      "affs": [
        1
      ],
      "name": "Xiaoyuan Yuan"
    },
    {
      "affs": [
        2
      ],
      "name": "Xiaoyuan Yuan"
    },
    {
      "affs": [
        0
      ],
      "name": "Wenwen Dong"
    },
    {
      "affs": [
        1
      ],
      "name": "Wenwen Dong"
    },
    {
      "affs": [
        2
      ],
      "name": "Wenwen Dong"
    },
    {
      "affs": [
        0
      ],
      "name": "Zhuoming Qin"
    },
    {
      "affs": [
        1
      ],
      "name": "Zhuoming Qin"
    },
    {
      "affs": [
        2
      ],
      "name": "Zhuoming Qin"
    },
    {
      "affs": [
        0
      ],
      "name": "Feng Hu"
    },
    {
      "affs": [
        1
      ],
      "name": "Feng Hu"
    },
    {
      "affs": [
        2
      ],
      "name": "Feng Hu"
    },
    {
      "affs": [
        0
      ],
      "name": "Kexiang Yu"
    },
    {
      "affs": [
        1
      ],
      "name": "Kexiang Yu"
    },
    {
      "affs": [
        2
      ],
      "name": "Kexiang Yu"
    },
    {
      "affs": [
        4
      ],
      "name": "Dzmitry Barysavets"
    },
    {
      "affs": [
        4
      ],
      "name": "Nasonau Ihar"
    },
    {
      "affs": [
        4
      ],
      "name": "Shchemialiova Natallia"
    },
    {
      "affs": [
        4
      ],
      "name": "Hongliang Wang"
    },
    {
      "affs": [
        0
      ],
      "name": "Guiming Li"
    },
    {
      "affs": [
        1
      ],
      "name": "Guiming Li"
    },
    {
      "affs": [
        2
      ],
      "name": "Guiming Li"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/c68qs8v8t6k0c.bib",
  "cited_by": 0,
  "doi": "10.3389/fcimb.2026.1978310",
  "fulltext_url": "https://www.frontiersin.org/articles/10.3389/fcimb.2026.1978310/full",
  "id": "c68qs8v8t6k0c",
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    "2235-2988"
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  "landing_url": "https://doi.org/10.3389/fcimb.2026.1978310",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
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  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
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  "pdf_url": "https://www.frontiersin.org/journals/cellular-and-infection-microbiology/articles/10.3389/fcimb.2026.1978310/pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-23",
  "publisher": "Frontiers Media S.A.",
  "ris": "https://research.draconitic.com/paper/c68qs8v8t6k0c.ris",
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      "first_seen": "2026-10-30T13:43:12Z",
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  "title": "Residue Gln370 of Newcastle disease virus nucleoprotein mediate viral inclusion body-like structure formation via interaction with residue Ser254 of viral phosphoprotein",
  "title_text": "Residue Gln370 of Newcastle disease virus nucleoprotein mediate viral inclusion body-like structure formation via interaction with residue Ser254 of viral phosphoprotein",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T13:43:12Z",
  "url": "https://research.draconitic.com/paper/c68qs8v8t6k0c",
  "venue": "Frontiers in Cellular and Infection Microbiology",
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