Overview:

The novel coronavirus SARS-CoV-2 has caused respiratory disease (COVID-19) pandemic around the world. The coronavirus spike glycoprotein (S) is a type I transmembrane protein that contains the S1 and S2 subunits and it interacts with the host cell angiotensin-converting enzyme 2 (ACE2) to facilitate viral genome entry (1). The Kappa variant (B.1.617.1 lineage) was first discovered in India and the mutations in the spike protein have reduced susceptibility to both monoclonal antibodies and convalescent plasma (2). Mutation E484Q increases the binding potential to ACE2 and mutation D614G increases viral infectivity (3). P681R mutation in the furin cleavage site promotes the cleavage rate of the S1-S2 making the virus more transmissible and more infectious (3). As new variants displace the first-wave virus, it is pivotal to evaluate their transmissibility, virulence, and their possible tendency to escape antibody neutralization (4).

Gene Aliases:

2019-nCoV s1, SARS-CoV-2 spike S1, SARS-CoV-2 S1, novel coronavirus spike s1, nCoV spike s1, SARS-CoV-2 Kappa variant

Genebank Number:

MN908947

Formulation:

Recombinant protein stored in 50mM sodium phosphate, pH 7.5, 300mM NaCl, 150mM imidazole

References:

1. Zhou P, et al: A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020, 579:270-89.

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: https://doi.org/10.1128/JCM.00741-21

3. Saito A, et al: SARS-CoV-2 spike P681R mutation enhances and accelerates viral fusion. bioRxiv. doi: https://doi.org/10.1101/2021.06.17.448820.

4. Starr TN, et al: Molecular dynamic simulation reveals E484Q mutation enhances spike RBD-ACE2 affinity and the combination of E484Q, 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.