February 17, 2021

501Y.V2 and 501Y.V3 Variants of SARS-CoV-2 Lose Binding to Bamlanivimab in Vitro

Category: Article Summary

Topic: Testing and Treatment

Keywords (Tags): treatment, variants

[Pre-print, not peer-reviewed] Three mutations found in the B.1.1.351 variant (first identified in South Africa) and the P1 variant (first identified in Brazil) completely abolished the interaction of monoclonal antibody treatment bamlanivimab with the receptor binding domain (RBD) of the virus.  Additionally, the K417N, E484K, and N501Y mutations found in the variants had higher binding affinity to the human ACE2 receptor compared to the wildtype RBD (about 2x higher) but less than the B.1.1.7 variant (~10 fold higher than wild-type). This suggests that variants containing these mutations may be more infectious than wild-type virus.  

Liu et al. (Feb 16, 2021). 501Y.V2 and 501Y.V3 Variants of SARS-CoV-2 Lose Binding to Bamlanivimab in Vitro. BioRxiv. https://doi.org/10.1101/2021.02.16.431305