{
  "abstract": "H1N1 influenza viruses have circulated continuously among human populations for five decades. During evolution, the hemagglutinin has accumulated amino acid substitutions in and around the receptor-binding site (RBS), mainly due to antigenic pressure, potentially altering receptor recognition and binding profiles. Here, we investigated the glycan-binding properties of H1N1 strains collected from 1977 through 2024 using ELISA, flow cytometry, and tissue histochemistry to characterize changes in receptor-binding specificity over time. Across the strains examined, we observe a recurring preference for binding 2,6-sialylated di-LacNAc N-glycans. Binding to 2,3-sialylated glycans was generally undetectable, although A/Hongkong/117/1977 and A/New Caledonia/20/1999 bind chicken tracheal tissues. Interestingly, post-pandemic H1N1 viruses fluctuate in their relative binding avidities. The responsible amino acids, in turn, have different effects in pre-pandemic HA proteins. We also report a classical egg-adapted H1N1 mutant that shows null binding across platforms. These findings highlight the contribution of RBS mutations during initial adaptation and evolution of human H1N1 influenza viruses to glycan-binding properties, which, in contrast to H3N2 viruses, never fail to bind glycans that correlate with avian erythrocyte hemagglutination.",
  "abstract_shown": true,
  "affiliations": [
    "Utrecht Institute for Pharmaceutical Sciences, Utrecht University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 7,
  "authors": [
    {
      "name": "R. Liang"
    },
    {
      "name": "J.-W. H. Langenbach"
    },
    {
      "name": "J. Kuo"
    },
    {
      "name": "A. Balas"
    },
    {
      "name": "M. Zobin"
    },
    {
      "name": "G.-J. Boons"
    },
    {
      "affs": [
        0
      ],
      "name": "R. P. de Vries"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/dcyxj248ax8m3.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.11.758004",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.11.758004v1.full",
  "id": "dcyxj248ax8m3",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.11.758004v1",
  "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",
      "microbiology"
    ],
    [
      "openalex",
      "2713|Influenza Virus Research Studies"
    ]
  ],
  "openalex": "W7221576807",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.11.758004v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-11",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/dcyxj248ax8m3.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:27:24Z",
      "native_id": "10.64898/2026.10.11.758004",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.11.758004v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:microbiology",
      "subfield": "microbiology"
    }
  ],
  "title": "Five decades of human H1N1 evolution reveal conserved glycan receptor specificity",
  "title_text": "Five decades of human H1N1 evolution reveal conserved glycan receptor specificity",
  "type": "preprint",
  "updated_at": "2026-10-30T12:27:24Z",
  "url": "https://research.draconitic.com/paper/dcyxj248ax8m3",
  "venue": "bioRxiv",
  "versions": []
}