{
  "abstract": "IntroductionInfluenza B virus is an important cause of seasonal influenza, with its contribution varying across regions and seasons. Historically, influenza B viruses have been classified into two major lineages: B/Victoria (BV) and B/Yamagata. No naturally circulating B/Yamagata-lineage viruses have been confirmed after March 2020, making protection against BV the current priority of influenza B vaccination. In our previous study, we demonstrated that the T214A mutation significantly alters the cross-neutralization capacity of this antigen, potentially through altered glycosylation. Notably, the WHO-recommended vaccine strain for the season, B/Austria/1359417/2021 (BV21), lacked the relevant glycosylation position.MethodsWe used an mRNA platform to compare the cross-subclade protection provided by B/Wyoming/06/2014 (BW06) and BV21 within the B/Victoria lineage. We also introduced the D212N substitution into BV21 as a minimal antigenic modification.ResultsThe D212N substitution restored the glycosylation motif in BV21 and enhanced cross-neutralizing responses against the tested heterologous strains. Mice immunized with a high dose of the D212N-modified vaccine showed 100% survival following challenge with the tested viruses from different subclades.DiscussionOur findings provide valuable insights for the development of broadly protective influenza B vaccines.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": "Original Research",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "Ziqi Cheng"
    },
    {
      "name": "Yeqing Sun"
    },
    {
      "name": "Yunbo Bai"
    },
    {
      "name": "Lan Wang"
    },
    {
      "name": "Chenyan Zhao"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/ecqdwn0eacewr.bib",
  "cited_by": 0,
  "doi": "10.3389/fmicb.2026.2002454",
  "fulltext_url": null,
  "id": "ecqdwn0eacewr",
  "issns": [
    "1664-302X"
  ],
  "landing_url": "https://www.frontiersin.org/articles/10.3389/fmicb.2026.2002454",
  "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": [
    [
      "feed-journal",
      "biology/microbiology"
    ]
  ],
  "openalex": null,
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-06",
  "publisher": "Frontiers Media SA",
  "ris": "https://research.draconitic.com/paper/ecqdwn0eacewr.ris",
  "sources": [
    {
      "first_seen": "2026-11-06T12:20:43Z",
      "native_id": "10.3389/fmicb.2026.2002454",
      "source": "feed-frontiers",
      "url": "https://www.frontiersin.org/articles/10.3389/fmicb.2026.2002454"
    },
    {
      "first_seen": "2026-11-06T12:21:13Z",
      "native_id": "10.3389/fmicb.2026.2002454",
      "source": "crossref",
      "url": "https://www.frontiersin.org/articles/10.3389/fmicb.2026.2002454/full"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "feed-journal:biology/microbiology",
      "subfield": "microbiology"
    }
  ],
  "title": "A glycosylation-associated hemagglutinin substitution improves the breadth of an influenza B mRNA vaccine",
  "title_text": "A glycosylation-associated hemagglutinin substitution improves the breadth of an influenza B mRNA vaccine",
  "type": "peer-reviewed",
  "updated_at": "2026-11-08T00:22:41Z",
  "url": "https://research.draconitic.com/paper/ecqdwn0eacewr",
  "venue": "Frontiers in Microbiology",
  "versions": []
}