Mutation detail:
| Mutation site | E484K/N501Y |
| 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 | Beta |
| Viral reference sequence | MN908947.3 |
| Drug/antibody/vaccine | STE90-C11-resistant |
| 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 | 34273271 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Cell Reports |
| Title | A SARS-CoV-2 neutralizing antibody selected from COVID-19 patients binds to the ACE2-RBD interface and is tolerant to most known RBD mutations |
| Author | Federico Bertoglio, Viola Fühner, Maximilian Ruschig, Philip Alexander Heine, Leila Abassi |
| Evidence | The antibody STE90-C11 showed reduced binding to N501Y and lost binding to K417N/K417T, but it was able to bind to all of the other investigated RBD mutations, including a S1-7PM mutant and more relevant to E484K, N439K, and L452R, which are the RBD mutations in the emerging B.1.525, B.1.526, B.1.1.33, B.1.258, and B.1.429/B.1.427 variants. |