Mutation detail:
| Mutation site | T345N |
| 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 | mAb_2H04 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 | 33535027 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Cell Host & Microbe |
| Title | Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization |
| Author | Zhuoming Liu, Laura A. VanBlargan, Louis-Marie Bloyet, Paul W. Rothlauf, Rita E. Chen |
| Evidence | Escape variants at residue E484 were isolated using 2B04, 1B07, SARS2-02, and SARS2-32, and specific substitutions at this residue led to varying degrees of resistance across the entire panel of antibodies. E484A exhibited a high degree of resistance to 2B04, 1B07, SARS2-01, SARS2-07, SARS2-19, SARS2-32, and SARS2-38; E484G exhibited resistance to 2B04, 1B07, SARS2-01, SARS2-32, and SARS2-38; E484K was resistant to 2B04, 1B07, SARS2-01, SARS2-02, SARS2-16, and SARS2-32; and E484D was resistant only to 1B07 (Figures 3A and S3). Substitution F486S was resistant to 2B04, 1B07, SARS2-07, SARS2-16, and SARS2-19, whereas F486Y exhibited resistance only to 1B07 and SARS2-16. Finally, substitution P499L was resistant to SARS2-07, SARS2-16, and SARS2-19. In addition to demonstrating that some mutations confer resistance to multiple neutralizing mAbs, these data suggest that each mAb recognizes distinct yet partially overlapping epitopes. |