Structural Characterization of a Neutralizing Nanobody With Broad Activity Against SARS-CoV-2 Variants.

ABSTRACT: SARS-CoV-2 and its variants, such as the Omicron continue to threaten public health. The virus recognizes the host cell by attaching its Spike (S) receptor-binding domain (RBD) to the host receptor, ACE2. Therefore, RBD is a primary target for neutralizing antibodies and vaccines. Here, we report the isolation and biological and structural characterization of a single-chain antibody (nanobody) from RBD-immunized alpaca. The nanobody, named DL28, binds to RBD tightly with a K _D of 1.56 nM and neutralizes the original SARS-CoV-2 strain with an IC₅₀ of 0.41 μg mL^-1. Neutralization assays with a panel of variants of concern (VOCs) reveal its wide-spectrum activity with IC₅₀ values ranging from 0.35 to 1.66 μg mL^-1 for the Alpha/Beta

SUBMITTER: Li T 

PROVIDER: S-EPMC9201380 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature