Mutation detail:
| Mutation site | V367F |
| 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 | - |
| Transmissibility |
promote |
| Transmission mechanism | Most interestingly, compared to WT RBD, the V367F, L452R, and Q493A RBD mutants obtained a three-to-five-fold increase in their binding to ACE2 (Figure 4B), suggesting that some of the RBD mutants indeed enhance the binding of the virus to its receptor, t |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| 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 | 34199601 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Viruses |
| Title | A Bioluminescent Biosensor for Quantifying the Interaction of SARS-CoV-2 and Its Receptor ACE2 in Cells and In Vitro |
| Author | Xiaolong Yang, Lidong Liu , Yawei Hao, Eva So, Sahar Sarmasti Emami, Derek Zhang |
| Evidence | figure4 |