{
  "abstract": "APOBEC3G (A3G), a restriction factor, is a barrier for zoonosis and targeted for degradation by the lentiviral protein Vif. Human Immunodeficiency Virus Type 1 (HIV-1) and HIV-2 arose from transmissions of lentiviruses from Old World monkeys to hominid primates. While HIV-1 Vif needed to adapt to specific residues in the arms race interface with A3G, HIV-2 Vif has greater tolerance for diversity there. Here, our cryo-EM structure of HIV-2 Vif and human A3G allows us to explore the mechanism underlying HIV-2 Vif broad specificity. While HIV-2 Vif does bind the arms race interface on A3G, HIV-2 Vif encodes tryptophans with low backbone stability to engage another interface on A3G. We propose a model where flexible loops in HIV-2 Vif undergo conformational selection to recognize diverse A3Gs, whereas the equivalent loops in HIV-1 Vif are preorganized to bind hA3G.",
  "abstract_shown": true,
  "affiliations": [
    "University of California, San Francisco"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "name": "E. K. Ronayne"
    },
    {
      "name": "M. Lilly"
    },
    {
      "name": "X. Lin"
    },
    {
      "name": "Y. Niu"
    },
    {
      "name": "N. M. Chesarino"
    },
    {
      "name": "M. Emerman"
    },
    {
      "name": "Y. Cheng"
    },
    {
      "affs": [
        0
      ],
      "name": "J. D. Gross"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/cv0tmqzpz4yt0.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.21.753272",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.21.753272v1.full",
  "id": "cv0tmqzpz4yt0",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.21.753272v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "2406|HIV Research and Treatment"
    ]
  ],
  "openalex": "W7214232401",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.21.753272v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-21",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/cv0tmqzpz4yt0.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:24:12Z",
      "native_id": "10.64898/2026.09.21.753272",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.21.753272v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Structural Adaptability in HIV-2 Vif Drives Broad Antagonism of APOBEC3G",
  "title_text": "Structural Adaptability in HIV-2 Vif Drives Broad Antagonism of APOBEC3G",
  "type": "preprint",
  "updated_at": "2026-10-30T12:24:12Z",
  "url": "https://research.draconitic.com/paper/cv0tmqzpz4yt0",
  "venue": "bioRxiv",
  "versions": []
}