Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escape.

ABSTRACT: An ideal anti-SARS-CoV-2 antibody would resist viral escape ^1-3 , have activity against diverse SARS-related coronaviruses ^4-7 , and be highly protective through viral neutralization ^8-11 and effector functions ^12,13 . Understanding how these properties relate to each other and vary across epitopes would aid development of antibody therapeutics and guide vaccine design. Here, we comprehensively characterize escape, breadth, and potency across a panel of SARS-CoV-2 antibodies targeting the receptor-binding domain (RBD), including S309 ⁴ , the parental antibody of the late-stage clinical antibody VIR-7831. We observe a tradeoff between SARS-CoV-2 in vitro neutralization potency and breadth of binding across SARS-related coronaviru

SUBMITTER: Starr TN 

PROVIDER: S-EPMC8043444 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature