Studying SARS-CoV-2 interactions using phage-displayed receptor binding domain as a model protein.

ABSTRACT: SARS-CoV-2 receptor binding domain (RBD) mediates viral entry into human cells through its interaction with angiotensin converting enzyme 2 (ACE2). Most neutralizing antibodies elicited by infection or vaccination target this domain. Such a functional relevance, together with large RBD sequence variability arising during viral spreading, point to the need of exploring the complex landscape of interactions between RBD-derived variants, ACE2 and antibodies. The current work was aimed at developing a simple platform to do so. Biologically active and antigenic Wuhan-Hu-1 RBD, as well as mutated RBD variants found in nature, were successfully displayed on filamentous phages. Mutational scanning confirmed the global plasticity of the receptor binding motif within RBD, highlighted residues playin

SUBMITTER: Perez-Masson B 

PROVIDER: S-EPMC10771503 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature