ArticleThe journal of physical chemistry. B2026
Mass Photometry Reveals Distinct ACE2 Binding Stoichiometries across SARS-CoV-2 Omicron Subvariants.
Article in The journal of physical chemistry. B, 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
Since late 2021, the SARS-CoV-2 Omicron variant has rapidly accumulated mutations in its spike (S) protein, leading to increased transmissibility and immune evasion. The COVID-19 pandemic caused by SARS-CoV-2 infections poses a significant global health challenge. While the binding affinity of Omicron S proteins to host receptor ACE2 has been extensively characterized, the binding stoichiometry across subvariants remains unclear. We used mass photometry (MP) to determine the ACE2 binding stoichiometry to different Omicron S subvariants. MP revealed diverse stoichiometries across subvariants, indicating that S protein mutations modulate ACE2 engagement beyond mere affinity. These findings reveal a nonlinear evolutionary trajectory of ACE2 engagement among Omicron subvariants, underscoring stoichiometry as a key variable in viral adaptation.
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