Mutation detail:
| Mutation site | A570D |
| 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 | Alpha |
| Viral reference sequence | NC 045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | Note that the downward displacement of SD2 was essentially governed by the downward loop movement promoted by the switch of salt bridge pairing that involves the A570D mutation. We propose that the switching of the A570D-mediated salt bridges may serve as |
| 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 | 34385690 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Nature Structural & Molecular Biology |
| Title | Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function |
| Author | Tzu-Jing Yang, Pei-Yu Yu, Yuan-Chih Chang, Kang-Hao Liang, Hsian-Cheng Tso |
| Evidence | To examine the contribution of the A570D mutation to viral infectivity, we generated a pseudovirus revertant, B.1.1.7+A570, in which the A570D mutation was restored into A570. Compared to B.1.1.7, the revertant was significantly more infectious in the pseudovirus assay (Fig. 3), suggesting that the A570D indeed plays a key role in modulating the RBD conformational transitions in the context of host infection. |