R Nutalai

TL;DR: In this paper, a structure-function analysis of B.1.351 was performed using a large cohort of convalescent and vaccinee serum samples, and it was shown that the receptor-binding domain mutations provide tighter ACE2 binding and widespread escape from monoclonal antibody neutralization largely driven by E484K, although K417N and N501Y act together against some important antibody classes.

TL;DR: In this paper, the ability of monoclonal antibodies and convalescent and vaccine sera to neutralize B.617.1 and B.1.2 has been studied.

TL;DR: In this paper, structural analysis of the ACE2 binding sites of the SARS-CoV-2 pandemic strain has been carried out and the authors show that the 222 light chain is able to largely restore neutralization potency to a major class of public antibodies.

TL;DR: In this article, the authors examined the ability of B.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination, and found that B. 1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light chain contacts with residue 501.

TL;DR: In this article, structural analysis of the SARS-CoV-2 pandemic showed that B.1.1 is significantly less resistant to naturally acquired or vaccine induced antibody responses.