Mutation detail:
| Mutation site | Y453F |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S |
| Gene ID | 43740568 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | Alpha |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Spike glycoprotein |
| Uniprot protein ID | P0DTC2 |
| Protein length | 1273 amino acids |
| Protein description | Spike protein is one of the structural proteins of SARS-CoV-2. The monomeric protein consists of one large ectodomain, a single-pass transmembrane anchor, and a short intracellular tail at C-terminus. It encompasses 22 glycosylation sites. S protein cleaves into two subunits namely S1 and S2 following receptor recognition. Receptor Binding Domain (RBD) in S1 subunit plays a major role in ACE2 receptor binding. |
Literature information:
| Pubmed ID | 34166617 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Cell Reports |
| Title | Recurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in the Alpha variant B.1.1.7 |
| Author | Bo Meng, Steven A Kemp, Guido Papa, Rawlings Datir, Isabella A T M Ferreira |
| Evidence | We therefore generated mutant spike plasmids bearing RBD mutations Y453F and N439K (Figure 5C) with and without delH69/V70 and performed infectivity assays in the lentiviral pseudotyping system. RBD mutations reduced infectivity of spike relative to the WT by around 2-fold (Figure 5D) and was partially rescued by delH69/V70. |