Overview:

The receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein recognizes the host ACE2 receptor and is a major determinant of viral entry and neutralization (1). SARS-CoV-2 variant, B.1.1.7 lineage, reported from the United Kingdom possess mutation N501Y at one of the six major contact residues in the receptor-binding domain involved in ACE2 binding. MD studies indicate that the mutant N501Y might increase the stability of the RBD domain with the ACE2 protein thereby resulting in higher virulence compared to the wild type strain (2). As 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. Sharma T, et al: Unbuttoning the impact of N501Y mutant RBD on viral entry mechanism: A computational insight. bioRxiv 2020; doi: https://doi.org/10.1101/2020.12.30.424906 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.