Overview:

The receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein that recognizes the host ACE2 receptor is a major determinant of viral entry and neutralization, and is also the most divergent region (1). SARS-CoV-2 spike variant with Y453F mutation has been associated with independent outbreaks linked to mink farms in the Netherlands and Denmark. Structure modeling studies have indicated relatively weaker binding of spike glycoprotein Y453F mutant to human ACE2 Spike protein and ability to escape four of the six tested monoclonal antibodies compared to wild type SARS-COV-2 (2). Hence, as the new variants displace the first-wave virus, it is pivotal to evaluate their transmissibility, virulence and their possible tendency to escape antibody neutralization (3).

Gene Aliases:

2019-nCoV RBD, SARS-CoV-2 spike RBD, novel coronavirus spike RBD, nCov spike RBD.

Genbank Number:

MN908947

References:

1. Lan J, et al: Crystal structure of the 2019-nCov spike receptor-binding domain bound with the ACE2 receptor. bioRxiv. doi: https://doi.org/10.1101/2020.02.19.956235.

2. Hayashi T, et al: Effect of RBD mutation (Y453F) in spike glycoprotein of SARS-CoV-2 on neutralizing antibody affinity. bioRxiv 2020; https://doi.org/10.1101/2020.11.27.401893.

3. Starr TN, et al: Molecular dynamic simulation reveals E484K mutation enhances spike RBD-ACE2 affinity and the combination of E484K, K417N and N501Y mutations (501Y.V2 variant) induces conformational change greater than N501Y mutant alone, potentially resulting in an escape mutant. Cell. 2020, 182(5):1295-1310.