Mutation detail:
| Mutation site | L452R |
| 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 | mAb_BD-368-2-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 | 32970990 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Cell |
| Title | Structurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy |
| Author | Shuo Du, Yunlong Cao, Qinyu Zhu, Pin Yu, Feifei Qi |
| Evidence | Four naturally occurring variants, L452R, V483A, V483I, and F490L were tested since Leu452, Val483, and Phe490 are critically involved in the BD-368-2/ RBD binding interface (Figures 6D and 6E). |