Mutation detail:
| Mutation site | Y453F |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S |
| Gene ID | 43740568 |
| Country | USA |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | casirivimab resisitant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| 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 | 33857422 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Cell Reports |
| Title | SARS-CoV-2 mutations acquired in mink reduce antibody-mediated neutralization |
| Author | Markus Hoffmann, Lu Zhang, Nadine Kruger, Luise Graichen, Hannah Kleine-Weber |
| Evidence | Importantly, mutation Y453F reduced inhibition by most serum/plasma samples tested, albeit with variable efficiency (median increase of serum/plasma titer required for 50% neutralization [NT50] = 1.62x, range = 1.02x to 3.43x), indicating that this RBD mutation may compromise SARS-CoV-2 control by preexisting neutralizing antibody responses (Figures 3A and S2).Similarly, the mutation Y453F reduced inhibition by one (casirivimab/REGN10933) out of a cocktail of two antibodies with EUA for COVID-19 therapy (REGN-CoV2), while an unrelated, non-neutralizing antibody was inactive (immunoglobulin G1 [IgG1]) (Figures 3B and S3). |