Mutation detail:
| Mutation site | D614G |
| 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 | MN908947.3 |
| Drug/antibody/vaccine | - |
| Transmissibility |
promote |
| Transmission mechanism | Here, we show that naturally occurring S mutations can reduce or enhance cell entry via ACE2 and TMPRSS2. A SARS-CoV-2 S-pseudotyped lentivirus exhibits substantially lower entry than that of SARS-CoV S. Among S variants, the D614G mutant shows the highes |
| 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 | 33558493 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Nature Communications |
| Title | SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity |
| Author | Seiya Ozono, Yanzhao Zhang, Hirotaka Ode, Kaori Sano, Toong Seng Tan |
| Evidence | we conclude that the D614G mutation increases cell entry by acquiring higher affinity to ACE2 while maintaining neutralization susceptibility. |