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 Haolin Liu
A1 Pengcheng Wei
A1 Qianqian Zhang
A1 Zhongzhou Chen
A1 Katja Aviszus
A1 Walter Downing
A1 Shelley Peterson
A1 Lyndon Reynoso
A1 Gregory P. Downey
A1 Stephen K. Frankel
A1 John Kappler
A1 Philippa Marrack
A1 Gongyi Zhang
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.