Mutation detail:
| Mutation site | E484K/R683G |
| 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_C933-resistant,mAb_C934-resistant,mAb_C129-resistant,mAb_C1003-resistant,mAb_C144-resistant,mAb_C871-resistant,mAb_C202-resistant,mAb_C006-resistant,mAb_C888-resistant,mAb_C153-resistant,mAb_C861-resistant,mAb_C853-resistant,mAb_C1008-resistant,mAb_C3 |
| 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 | 34126625 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Nature |
| Title | Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection |
| Author | Zijun Wang, Frauke Muecksch, Dennis Schaefer-Babajew, Shlomo Finkin, Charlotte Viant |
| Evidence | Fig 4 |