Mutation detail:
| Mutation site | K417T |
| 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 | |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | The substitution of lysine417 to either an asparagine (K417N) or a threonine (K417T) results in a significant reduction in RBD/ACE-2 affinity, while the N501Y confers a ten-fold affinity increase towards ACE-2 |
| 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 | 34691078 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Frontiers in Immunology |
| Title | Functional Effects of Receptor-Binding Domain Mutations of SARS-CoV-2 B.1.351 and P.1 Variants |
| Author | Rafael Bayarri-Olmos, Ida Jarlhelt, Laust Bruun Johnsen, Cecilie Bo Hansen, Charlotte Helgstrand |
| Evidence | The same three positions in the receptor-binding domain (RBD) are affected in both variants, but where the 417 substitution differs, the E484K/N501Y have co-evolved by convergent evolution. |