Overview:

The novel coronavirus SARS-CoV-2 (COVID-19) has caused a respiratory disease pandemic worldwide since 2020. The coronavirus spike glycoprotein (S) is a type I transmembrane protein that contains the S1 and S2 subunits and interacts with the host cell angiotensin converting enzyme 2 (ACE2) to facilitate viral genome entry (1). The IHU variant (B.1.640.2 lineage) was first discovered in southern France, and out of the total 30 amino acid substitutions and 12 deletions in the IHU variant, 14 substitutions and 9 deletions are located in the spike protein. Several of the detected mutations were predicted to significantly affect neutralizing epitopes (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 s1, SARS-CoV-2 spike S1, SARS-CoV-2 S1, novel coronavirus spike s1, nCoV spike s1, coronavirus spike S1.

Genebank Number:

MN908947

References:

1. Lan J, et al: Crystal structure of the 2019-nCov spike receptor-binding domain bound with the ACE2 receptor. Nature. 2020, 581:215-220.
2. Colson, P. et al. Emergence in Southern France of a new SARS-CoV-2 variant of probably Cameroonian origin harbouring both substitutions N501Y and E484K in the spike protein. medRxiv 2021; https://doi.org/10.1101/2021/12/24/21268174.
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.