{
  "abstract": "The protein C is a small viral protein encoded in an overlapping frame of the P gene in the subfamily Orthoparamyxovirinae. This protein, expressed by alternative translation initiation, is a virulence factor that regulates viral transcription, replication, and production of defective interfering RNA, interferes with the host-cell innate immunity systems and supports the assembly of viral particles and budding. We expressed and purified full-length and an N-terminally truncated C protein from Tupaia paramyxovirus (TupV) C protein (genus Narmovirus). We solved the crystal structure of the C-terminal part of TupV C protein at a resolution of 2.4 Å and found that it is structurally similar to Sendai virus C protein, suggesting that despite undetectable sequence conservation, these proteins are homologous. We characterized both truncated and full-length proteins by SEC-MALLS and SEC-SAXS and described their solution structures by ensemble models. We established a minireplicon assay for the related Nipah virus (NiV) and showed that TupV C inhibited the expression of NiV minigenome in a concentration-dependent manner as efficiently as the NiV C protein. A previous study found that the Orthoparamyxovirinae C proteins form two clusters without detectable sequence similarity, raising the question of whether they were homologous or instead had originated independently. Since TupV C and SeV C are representatives of these two clusters, our discovery that they have a similar structure indicates that all Orthoparamyxovirine C proteins are homologous. Our results also imply that, strikingly, a STAT1-binding site is encoded by exactly the same RNA region of the P/C gene across Paramyxovirinae, but in different reading frames (P or C), depending on which cluster they belong to.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 11,
  "authors": [
    {
      "name": "Ada Roy"
    },
    {
      "name": "Emeric Chan Mine"
    },
    {
      "name": "Lorenzo Gaifas"
    },
    {
      "name": "Cédric Leyrat"
    },
    {
      "name": "Valentina A Volchkova"
    },
    {
      "name": "Florence Baudin"
    },
    {
      "name": "Luis Martinez-Gil"
    },
    {
      "name": "Viktor E Volchkov"
    },
    {
      "name": "David G Karlin"
    },
    {
      "name": "Jean-Marie Bourhis"
    },
    {
      "name": "Marc Jamin"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/0txap6cedavkw.bib",
  "cited_by": 7,
  "doi": "10.3390/biom13030455",
  "fulltext_url": null,
  "id": "0txap6cedavkw",
  "issns": [
    "2218-273X"
  ],
  "landing_url": "https://hal.science/hal-05796746v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.sdv.mp"
    ],
    [
      "hal",
      "2.sdv.mp.vir"
    ],
    [
      "openalex",
      "2713|Virology and Viral Diseases"
    ]
  ],
  "openalex": "W4322769627",
  "pdf_url": "https://hal.science/hal-05796746/document",
  "pmcid": null,
  "pmid": "36979390",
  "published": "2026-10-13",
  "publisher": "MDPI",
  "ris": "https://research.draconitic.com/paper/0txap6cedavkw.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:55Z",
      "native_id": "hal-05796746",
      "source": "hal",
      "url": "https://hal.science/hal-05796746v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "hal:1.sdv.mp",
      "subfield": "microbiology"
    }
  ],
  "title": "Orthoparamyxovirinae C Proteins Have a Common Origin and a Common Structural Organization",
  "title_text": "Orthoparamyxovirinae C Proteins Have a Common Origin and a Common Structural Organization",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:55Z",
  "url": "https://research.draconitic.com/paper/0txap6cedavkw",
  "venue": "Biomolecules",
  "versions": []
}