Journal of virology · 2023
Cryptic-site-specific antibodies to the SARS-CoV-2 receptor binding domain can retain functional binding affinity to spike variants.
СтатьяПоддержка NIH: внешняя программаПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод пока не подготовлен
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Li Kan, Huntwork Richard H C, Horn Gillian Q, Abraha Milite, Hastie Kathryn M, Li Haoyang, Rayaprolu Vamseedhar, Olmedillas Eduardo, Feeney Elizabeth, Cronin Kenneth, Schendel Sharon L, Heise Mark, Bedinger Daniel, Mattocks Melissa D, Baric Ralph S, Alam S Munir, Saphire Erica Ollmann, Tomaras Georgia D, Dennison S Moses
Аннотация
Multiple SARS-CoV-2 variants of concern have emerged and caused a significant number of infections and deaths worldwide. These variants of concern contain mutations that might significantly affect antigen-targeting by antibodies. It is therefore important to further understand how antibody binding and neutralization are affected by the mutations in SARS-CoV-2 variants. We highlighted how antibody epitope specificity can influence antibody binding to SARS-CoV-2 spike protein variants and neutralization of SARS-CoV-2 variants. We showed that weakened spike binding and neutralization of Beta (B.1.351) and Omicron (BA.1) variants compared to wildtype are not universal among the panel of antibodies and identified antibodies of a specific binding footprint exhibiting consistent enhancement of spike binding and retained neutralization to Beta variant. These data and analysis can inform how antigen-targeting by antibodies might evolve during a pandemic and prepare for potential future sarbecovirus outbreaks.