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<p>Influenza A H5N1 is a flu strain capable of causing avian, human, and mammalian infections with the receptor binding domain (RBD) of the hemagglutinin (HA) protein playing a key role in determining host susceptibility. The influenza A H5N1 HA protein undergoes multiple mutations all throughout HA protein evolution that can either generate diversity or loss of function which in-turn affects viral pathogenicity since these mutations can generate functional diversity and/or functional loss. Thus, establishing the HA structural similarities ascribable to functional protein mutations during HA protein evolution becomes important since this may help determine cross-species infection. Here, we generated HA protein models of the 2001–2024 H5N1 avian, human, and mammalian strains using an AI platform. Subsequently, we determined the HA RBD structural dynamics measurements and identified the amino acid residues that are able to alter these measurements. We found that the 2024 avian, human, and mammalian HA protein models share structural similarities and exhibit similar HA RBD structural dynamics possibly resulting in cross-species infection. Additionally, we highlighted the potential role of residues 115 and 195 in the evolution of the 2024 H5N1 HA protein from the 2022 H5N1 HA protein possibly attributable to viral protein reversion.</p>

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Structural comparison of the influenza A H5N1 hemagglutinin protein models across the 2001–2024 strains reveals cross-species similarity in the 2024 avian, human, and mammalian variants

  • 期刊论文

  • 发表日期：

    2026年2月4日

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  • Marni E. Cueno,
  • Kenichi Imai

摘要

Influenza A H5N1 is a flu strain capable of causing avian, human, and mammalian infections with the receptor binding domain (RBD) of the hemagglutinin (HA) protein playing a key role in determining host susceptibility. The influenza A H5N1 HA protein undergoes multiple mutations all throughout HA protein evolution that can either generate diversity or loss of function which in-turn affects viral pathogenicity since these mutations can generate functional diversity and/or functional loss. Thus, establishing the HA structural similarities ascribable to functional protein mutations during HA protein evolution becomes important since this may help determine cross-species infection. Here, we generated HA protein models of the 2001–2024 H5N1 avian, human, and mammalian strains using an AI platform. Subsequently, we determined the HA RBD structural dynamics measurements and identified the amino acid residues that are able to alter these measurements. We found that the 2024 avian, human, and mammalian HA protein models share structural similarities and exhibit similar HA RBD structural dynamics possibly resulting in cross-species infection. Additionally, we highlighted the potential role of residues 115 and 195 in the evolution of the 2024 H5N1 HA protein from the 2022 H5N1 HA protein possibly attributable to viral protein reversion.