{
  "abstract": "The HIV-1 capsid, composed of capsid (CA) proteins arranged into a conical surface lattice, serves as a critical platform for host–pathogen interactions. Many host cofactors regulate HIV-1 infection by selectively recognizing the higher-order CA lattice rather than individual monomers or capsomers. Among these, Myxovirus resistance protein B (MxB) is a key cellular restriction factor that binds the capsid via its N-terminal fragment containing an arginine-rich motif (RRR), blocking HIV-1 infection at early infection stages. However, the structural basis of this interaction has remained elusive. Here, we present a structural characterization of the CA lattice in complex with the MxB N-terminal fragment using cryo-electron tomography and subtomogram averaging. Combining cryoEM structures with EM-guided all-atom molecular dynamics simulations, we identify residue-specific interactions between MxB and the CA trimer interfaces. Notably, residues 10-20 of the MxB N-terminus adopt an α-helical conformation that stabilizes binding at the CA trimer interface, revealing a distinct mode of capsid engagement. These findings provide insight into arginine-rich motif–mediated recognition by MxB and other host factors and establish a structural framework for the development of capsid-targeting antiviral therapeutics.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "Yanan Zhu",
      "orcid": "0000-0003-1025-7929"
    },
    {
      "name": "Juan S. Rey",
      "orcid": "0000-0003-2274-3748"
    },
    {
      "name": "Juan Shen",
      "orcid": "0000-0002-1883-3057"
    },
    {
      "name": "Juan R. Perilla",
      "orcid": "0000-0003-1171-6816"
    },
    {
      "name": "Peijun Zhang",
      "orcid": "0000-0003-1803-691X"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/a5cw6kd3417e5.bib",
  "cited_by": 0,
  "doi": "10.1038/s41467-026-78493-x",
  "fulltext_url": null,
  "id": "a5cw6kd3417e5",
  "issns": [
    "2041-1723"
  ],
  "landing_url": "https://www.nature.com/articles/s41467-026-78493-x",
  "language": null,
  "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": [
    [
      "openalex",
      "2406|HIV Research and Treatment"
    ]
  ],
  "openalex": "W7222754567",
  "pdf_url": "https://www.nature.com/articles/s41467-026-78493-x_reference.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-16",
  "publisher": "Springer Science and Business Media LLC",
  "ris": "https://research.draconitic.com/paper/a5cw6kd3417e5.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:38Z",
      "native_id": "10.1038/s41467-026-78493-x",
      "source": "crossref",
      "url": "https://www.nature.com/articles/s41467-026-78493-x"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:2406|HIV Research and Treatment",
      "subfield": "microbiology"
    }
  ],
  "title": "MxB N-terminus adopts a stable α-helix to engage the HIV-1 capsid trimer interface",
  "title_text": "MxB N-terminus adopts a stable α-helix to engage the HIV-1 capsid trimer interface",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:38Z",
  "url": "https://research.draconitic.com/paper/a5cw6kd3417e5",
  "venue": "Nature Communications",
  "versions": []
}