Overview:

Novel coronavirus SARS-CoV-2 has caused the pandemic of the respiratory diseases (COVID-19) around the world since 2020 (1). The spike glycoprotein (S) of coronavirus binds to the host cells through the interaction with angiotensin-converting enzyme 2 (ACE2) and facilitate viral entry into the host cell (2). SARS-CoV-2 (501Y.V2 variant) with mutations K417N, E484K and N501Y in the spike protein severely affected regions of South Africa (2). A combination of E484K, K417N and N501Y results in the highest degree of conformational modifications of receptor binding domain of spike protein when bound to hACE2, compared to either E484K or N501Y alone. E484K and N501Y increase affinity of RBD for hACE2 and the charge switch due to E484K leads to the formation of favorable contacts (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

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. Houriiyah T, et al: Emergence and rapid spread of a new severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) lineage with multiple spike mutations in South Africa. medRxiv 2020; doi: https://doi.org/10.1101/2020.12.21.20248640 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 4. Harvey WT, et al: SARS-CoV-2 variants, spike mutations and immune escape. Nat Rev. Microbiol. 2021, 19:409–424.