Mutation detail:
| Mutation site | V213A |
| 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 | mAb_8D2-resistant,mAb_COV2-2210-resistant,mAb_COV2-2369-resistant,mAb_COV2-2490-resistant,mAb_COV2-2660-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 | 34139176 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | cell |
| Title | An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies |
| Author | Yafei Liu, Wai Tuck Soh, Jun-Ichi Kishikawa, Mika Hirose, Emi E Nakayama |
| Evidence | We then analyzed a series of NTD mutants in which amino acid residues structurally close to R214 or K187 were mutated to alanine and found that binding of enhancing antibodies to the NTD was substantially decreased in W64A, H66A, K187A, V213A, and R214A mutants (Figure 4B). |