Mutation detail:
| Mutation site | N501Y/E484K |
| 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 | - |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | bamlanivimab 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 | 34074219 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | mAbs |
| Title | 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro |
| Author | Haolin Liu,Pengcheng Wei,Qianqian Zhang,Zhongzhou Chen,Katja Aviszus |
| Evidence | To our surprise, the interaction between the mutant RBD containing three mutations, N417/K484/Y501-RBD, and bamlanivimab, was completely abolished (Figure 2(a)). However, the binding between N417/Y501-RBD and antibody remains the same as those between wildtype N501-RBD or mutated Y501-RBD and the antibody with binding affinities of 0.976 nM (Figure 2(b)), 0.874 nM and 0.801 nM, respectively.Furthermore, when the E484K mutation is introduced, the binding between K484/Y501-RBD and the antibody is completely abolished (Figure 2(a) and (c)). |