Mutation detail:
| Mutation site | L452R |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S |
| Gene ID | 43740568 |
| Country | USA,Mexico |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC 045512.2 |
| Drug/antibody/vaccine | patrient convalescent plasma-resistant |
| Transmissibility |
promote |
| Transmission mechanism | Although the L452 residue is not directly located at the binding interface (Figure 2A), structural analysis and in silico mutagenesis suggest that the L452R substitution promotes electrostatic complementarity (Selzer et al., 2000) (Figure 2G).Because resi |
| 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 | 34171266 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Cell Host & Microbe |
| Title | SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity |
| Author | Chihiro Motozono, Mako Toyoda, Jiri Zahradnik, Akatsuki Saito, Hesham Nasser |
| Evidence | Here, we demonstrate that two recently emerging mutations in the receptor-binding domain of the SARS-CoV-2 spike protein, L452R (in B.1.427/429 and B.1.617) and Y453F (in B.1.1.298), confer escape from HLA-A24-restricted cellular immunity. These mutations reinforce affinity toward the host entry receptor ACE2. |