501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to Bamlanivimabin vitro

Haolin Liu,Pengcheng Wei,Qianqian Zhang,Zhongzhou Chen,Katja Aviszus,Walter Downing,Shelley Peterson,Lyndon Reynoso,Gregory P. Downey, Stephen K. Frankel,John Kappler,Philippa Marrack,Gongyi Zhang

bioRxiv (Cold Spring Harbor Laboratory)（2021）

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摘要

AbstractWe generated several versions of the receptor binding domain (RBD) of the Spike protein with mutations existing within newly emerging variants from South Africa and Brazil. We found that the mutant RBD with K417N, E484K, and N501Y exchanges has higher binding affinity to the human receptor compared to the wildtype RBD. This mutated version of RBD also completely abolishes the binding to a therapeutic antibody, Bamlanivimab,in vitro.

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bamlanivimab<i>in,sars-cov

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