Overview:

The receptor binding domain (RBD) of SARS-CoV-2 spike glycoprotein can recognize the ACE2 receptor of the host and is an important determining factor of viral entry and neutralization (1). The SARS-CoV-2 variant C.1.2 carries the mutations Y449H, E484K, and N501Y on its RBD and these mutations together manifest resistance to antiviral immunity. Virus with C.1.2 spike is more resistant to antibody neutralization than any variants of concern (VOCs) (2). As more virus emerge, it is pivotal to study the transmissibility, virulence, and their possible tendency to escape antibody neutralization of the virus (3).

Gene Aliases:

2019-nCoV RBD, SARS-CoV-2 spike RBD, novel coronavirus spike RBD, nCoV spike RBD, SARS-CoV-2 variant C.1.2.

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. Tada T, et al: Neutralization of Mu and C. 1.2 SARS-CoV-2 Variants by Vaccine-elicited Antibodies in Individuals With and Without Previous History of Infection. bioRxiv. doi: https://doi.org/10.1101/2021.10.19.463727

3. Starr TN, et al: Molecular dynamic simulation reveals E484K mutation enhances spike RBD-ACE2 affinity and the combination of E484K, K417T 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.