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- W4221120989 abstract "The COVID-19 pandemic resulting from the spread of SARS-CoV-2 spurred devastating health and economic crises around the world. Neutralizing antibodies and licensed vaccines were developed to combat COVID-19, but progress was slow. In addition, variants of the receptor-binding domain (RBD) of the spike protein confer resistance of SARS-CoV-2 to neutralizing antibodies, nullifying the possibility of human immunity. Therefore, investigations into the RBD mutations that disrupt neutralization through convalescent antibodies are urgently required. In this study, we comprehensively and systematically investigated the binding stability of RBD variants targeting convalescent antibodies and revealed that the RBD residues F456, F490, L452, L455, and K417 are immune-escaping hotspots, and E484, F486, and N501 are destabilizing residues. Our study also explored the possible modes of actions of emerging SARS-CoV-2 variants. All results are consistent with experimental observations of attenuated antibody neutralization and clinically emerging SARS-CoV-2 variants. We identified possible immune-escaping hotspots that could further promote resistance to convalescent antibodies. The results provide valuable information for developing and designing novel monoclonal antibody drugs to combat emerging SARS-CoV-2 variants." @default.
- W4221120989 created "2022-04-03" @default.
- W4221120989 creator A5006986887 @default.
- W4221120989 creator A5010982545 @default.
- W4221120989 creator A5044667117 @default.
- W4221120989 creator A5066252111 @default.
- W4221120989 date "2022-03-22" @default.
- W4221120989 modified "2023-10-01" @default.
- W4221120989 title "Antigen–Antibody Complex-Guided Exploration of the Hotspots Conferring the Immune-Escaping Ability of the SARS-CoV-2 RBD" @default.
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- W4221120989 doi "https://doi.org/10.3389/fmolb.2022.797132" @default.
- W4221120989 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35392535" @default.
- W4221120989 hasPublicationYear "2022" @default.
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