ArticleJournal of virology2025
The hemagglutinin proteins of clades 1 and 2.3.4.4b H5N1 highly pathogenic avian influenza viruses exhibit comparable attachment patterns to avian and mammalian tissues.
Article in Journal of virology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Novel emerging reassortant H6 avian influenza viruses with internal genes from G57 genotype of H9N2 pose potential zoonotic risk.Emerging microbes & infections · 2026Article
- Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.Journal of virology · 2026Article
- H5N1 influenza binding and cell entry via human class II MHC, and blocking by cross-reactive antibodies.bioRxiv : the preprint server for biology · 2026Article
- A cross-sectional study of avian influenza virus in poultry markets of Guangdong China, 2025.Frontiers in cellular and infection microbiology · 2026Article
- Influenza A Virus H5N1 Subtype: Resurgent Interspecies and Intercontinental Transmission, and a New Host.Pathogens (Basel, Switzerland) · 2025Review
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Abstract
The global spread of the A/goose/Guangdong/1/96-lineage H5N1 highly pathogenic avian influenza (HPAI) viruses has been accompanied by an expanded host range and the establishment of sustained viral transmission among dairy cattle. To evaluate if the evolving H5N1 viruses have changed tissue tropism over time, we compared the binding patterns of recombinant hemagglutinin (HA) proteins derived from clade 1 (A/Vietnam/1203/04, H5VN) and circulating clade 2.3.4.4b viruses detected from wild bird (A/Eurasian Teal/Hong Kong/AFCD-HKU-23-14009-01020/2023, H5HK) and dairy cattle (A/bovine/Ohio/B24OSU-439/2024, H5OH). The HA protein of A(H1N1)pdm09 virus was included for comparison. Using bio-layer interferometry, H1 protein preferentially bound to the α2,6-linked sialoside 6'SLNLN, while H5 proteins preferentially bound to the α2,3-linked sialoside 3'SLN. H5OH showed higher binding affinity to 3'SLN than H5HK and H5VN. The attachment patterns of H1 and H5 proteins to the respiratory tissues of different species and dairy cattle mammary glands were evaluated. Compared to the H1 protein, H5 proteins showed stronger binding to the lung epithelial cells of cat, cattle, chicken, ferret, human, and pig, and the clade 2.3.4.4b H5 proteins exhibited increased binding to pig and cattle bronchial epithelial cells. All H5 proteins were attached to the alveolar and cistern epithelial cells in mammary glands, where α2,3-linked and α2,6-linked sialyl glycans were detected by IMPORTANCE: The outbreaks of H5N1 highly pathogenic avian influenza (HPAI) virus among US dairy cattle since 2024 have raised concerns of the potential changes in HA receptor binding specificity and tissue tropism. Using insect-cell-expressed recombinant HA proteins derived from clade 1 and circulating clade 2.3.4.4b H5N1 viruses, we showed that the dairy cattle H5 protein retained binding specificity for the avian-like α2,3-linked sialoside 3'SLN over the human-like α2,6-linked sialoside 6'SLNLN, with higher binding affinity to 3'SLN than the other H5 proteins. Clade 1 and 2.3.4.4b H5 proteins showed comparable attachment patterns to the mammary tissues of lactating dairy cattle, which showed high expression of α2,3-linked and α2,6-linked sialyl glycans. All H5 proteins also showed comparable attachment patterns to the lungs of cat, cattle, chicken, ferret, human, and pig. Our results suggest that the recent H5N1 outbreaks in dairy cattle may be related to ecological factors rather than changes in HA receptor binding specificity.
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