PT  - JOURNAL ARTICLE
AU  - Liu, Haolin
AU  - Wei, Pengcheng
AU  - Zhang, Qianqian
AU  - Chen, Zhongzhou
AU  - Aviszus, Katja
AU  - Downing, Walter
AU  - Peterson, Shelley
AU  - Reynoso, Lyndon
AU  - Downey, Gregory P.
AU  - Frankel, Stephen K.
AU  - Kappler, John
AU  - Marrack, Philippa
AU  - Zhang, Gongyi
TI  - 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to Bamlanivimab <em>in vitro</em>
AID  - 10.1101/2021.02.16.431305
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.02.16.431305
4099  - http://biorxiv.org/content/early/2021/02/16/2021.02.16.431305.short
4100  - http://biorxiv.org/content/early/2021/02/16/2021.02.16.431305.full
AB  - We 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.Competing Interest StatementH.L. is partially supported by NB Life Laboratory LLC, G.Z. holds equity at NB Life Laboratory LLC. We do not have any financial relation with Pfizer-BioNTech, Moderna, Eli Lilly, or Regeneron.