ArticleArchives of virology2026
Functional and structural characterization of the SARS-CoV-2 spike N481K mutation.
Article in Archives of virology, 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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Abstract
backgroundSelective pressure drives SARS-CoV-2 evolution, with spike RBD substitutions shaping ACE2 binding and antibody escape. N481K RBD mutation emerged early in Qatar (2020) and later re-emerged globally, reaching near-fixation by 2024-2025, yet its functional significance remained unexplored.
methodsWe analyzed the temporal and geographic circulation of N481K across > 17 million SARS-CoV-2 genomes (2020-2025). Structural effects were assessed using modeling, docking, and molecular dynamics. Functional impact was evaluated using VSV pseudovirus neutralization tests with sera from infected individuals (n = 48) and vaccinated cohorts: mRNA (n = 16), Sinopharm (n = 45), and AstraZeneca (n = 28).
resultsN481K was detected in 4.14% (703,777/17,016,111) of global genomes and reached near-fixation (> 90%) in dominant Omicron lineages by 2024, with prevalence rising from 71.5% in early 2024 to 94.4% by week 36 of 2025. Structural analyses showed a 0.706 Å RMSD deviation and higher ACE2 docking affinity (-313 vs. - 308 kcal/mol) compared to the wild-type (WT) RBD. Molecular dynamics confirmed increased stability and lower binding free energy for N481K versus WT (-77.07 ± 0.90 vs. - 43.09 ± 0.98 kcal/mol). Among samples with detectable WT neutralization (n = 89), mean neutralization declined from 69.76% (WT) to 42.47% (N481K) (p < 0.0001), with the largest reductions in AstraZeneca, Sinopharm, and infected cohorts. mRNA recipients retained the highest neutralization [77.5% (WT) vs. 56.0% (N481K)].
conclusionN481K enhances ACE2 binding while partially evading antibody neutralization, suggesting viral fitness and persistence.
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