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?:abstract
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Antibody cocktails represent a promising approach to prevent SARS-CoV-2 escape. The determinants for selecting antibody combinations and the mechanism that antibody cocktails prevent viral escape remain unclear. We compared the critical residues in the receptor-binding domain (RBD) used by multiple neutralizing antibodies and cocktails and identified a combination of two antibodies CoV2-06 and CoV2-14 for preventing viral escape. The two antibodies simultaneously bind to non-overlapping epitopes and independently compete for receptor binding. SARS-CoV-2 rapidly escapes from individual antibodies by generating resistant mutations in vitro, but it doesn’t escape from the cocktail due to stronger mutational constraints on RBD-ACE2 interaction and RBD protein folding requirements. We also identified a conserved neutralizing epitope shared between SARS-CoV-2 and SARS-CoV for antibody CoV2-12. Treatments with CoV2-06 and CoV2-14 individually and in combination confer protection in mice. These findings provide insights for rational selection and mechanistic understanding of antibody cocktails as candidates for treating COVID-19.
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?:doi
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10.1038/s41467-020-20789-7
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document_parses/pdf_json/e534b94a3aef598ca0c1fc5b232eaf1adde79364.json; document_parses/pdf_json/c79aa1803da9e2a45dc8a043c024129df908f891.json
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document_parses/pmc_json/PMC7817669.xml.json
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?:source
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?:title
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Molecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape
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