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 the most divergent region (1). L452R mutation has been previously reported in the California variant (B1.429). Mutation at E484 has been detected in the South African (B.1.351), Brazilian (P.1), and NY variants (B.1.526). Lineage B.1.617, also known as the Indian variant carries unique combination of both E484Q and L452R mutations in the RBD of the spike protein. Viruses harboring these individual mutations have reduced susceptibility to both monoclonal antibodies and convalescent plasma (2). As these 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, Kappa

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. Verghese M, et al: Identification of a SARS-CoV-2 variant with L452R and E484Q neutralization resistance mutations. J Clin Microbiol. 2021, JCM.00741-21. doi: 10.1128/JCM.00741-21 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.