Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.

ABSTRACT: Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu⁴⁸⁴, Lys⁴¹⁷, and Asn⁵⁰¹ are mutated in variants first described in South Africa (B.1.351) and Brazil (P.1). We analyzed their effects on angiotensin-converting enzyme 2 binding, as well as the effects of two of these mutations (K417N and E484K) on nAbs isolated from COVID-19 patients. Binding and neutralization of the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2), which can both bind the RBS in alternative binding modes, are abrogated by K417N, E484K, or both. These effects can

SUBMITTER: Yuan M 

PROVIDER: S-EPMC8284396 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature