RT Journal Article
SR Electronic
T1 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to Bamlanivimab <em>in vitro</em>
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.02.16.431305
DO 10.1101/2021.02.16.431305
A1 Liu, Haolin
A1 Wei, Pengcheng
A1 Zhang, Qianqian
A1 Chen, Zhongzhou
A1 Aviszus, Katja
A1 Downing, Walter
A1 Peterson, Shelley
A1 Reynoso, Lyndon
A1 Downey, Gregory P.
A1 Frankel, Stephen K.
A1 Kappler, John
A1 Marrack, Philippa
A1 Zhang, Gongyi
YR 2021
UL http://biorxiv.org/content/early/2021/02/16/2021.02.16.431305.abstract
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.