ArticleJournal of veterinary science2026
Genome-informed structural analysis of polymerase and glycoprotein adaptation in H5N1 clade 2.3.4.4b.
Article in Journal of veterinary science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
importanceUnderstanding the molecular mechanisms driving H5N1 clade 2.3.4.4b is critical for pandemic preparedness.
objectiveTo characterize the molecular drivers of viral fitness and mammalian adaptability in recent H5N1 viruses by integrating evolutionary dynamics with structural simulations.
methodsThis study analyzed 2,398 H5Nx genomes (2000-2024) through phylogenetic and selective pressure analyses. HA/NA structures were predicted with AlphaFold 3 and evaluated by AutoDock4 docking, whereas polymerase-ANP32A/B complexes were modeled using template-based methods and their binding free energies were estimated using MM/GBSA. Polymerase-ANP32E complexes were predicted with AlphaFold 3 and similarly evaluated by MM/GBSA. The binding affinities (ΔG) for the sialic acid (SA) receptors and human ANP32 proteins were quantified through molecular mechanics/generalized born surface area calculations.
resultsClade 2.3.4.4b showed significant antigenic drift in the HA receptor binding site, reducing affinity for CONCLUSIONS AND RELEVANCE: The co-occurrence of HA, NA, PB1, and PB2 signatures was associated with clade expansion and produced structural predictions consistent with altered receptor or ANP32 interactions; experimental validation is required before inferring effects on fitness or zoonotic risk.
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