Overview:

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) remains the most rapidly spreading disease since 2020. The spike glycoprotein (S) of coronavirus, a type I transmembrane protein containing two subunits S1 and S2, facilitates viral genome entry into the host cells through the interaction with angiotensin-converting enzyme 2 (ACE2) (1). The B.1.621 variant emerged from the parental B.1 lineage. It was first found in Colombia in January 2021, and the World Health Organization (WHO) designated the variant as Mu in August 2021(2). Compared to Delta, the Mu variant shows enhanced immune resistance to antibodies, and the E484K mutation, an escape mutation, is considered to be the reason for reducing the neutralizing ability of antibodies (3). As more variants of the virus emerge, it is pivotal to study the transmissibility, virulence, and their possible tendency to escape antibody neutralization of the virus (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 Mu variant.

Genbank 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. Xiochun, X, et al. "Emerging SARS-CoV-2 B. 1.621/Mu variant is prominently resistant to inactivated vaccine-elicited antibodies." Zoological Research 42 (2021): 1-3.

3. Harvey, W.T, et al. SARS-CoV-2 variants, spike mutations and immune escape. Nat Rev Microbiol. 2021, 19: 409–424.

4. 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