Mutation detail:
| Mutation site | Y442S |
| Virus | SARS-CoV |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S protein |
| Gene ID | 1489668 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | |
| Viral reference sequence | AY278741.1 |
| Drug/antibody/vaccine | nAb Y12 resistant |
| Transmissibility |
promote |
| Transmission mechanism | Although most of the mutations occurred at positions at the RBD-hACE2 interface (48), they did not appreciably change the binding affinity (KD) and kinetics (Kon and Koff) to hACE2, except Y12's escape mutation (Y442S), which had an ∼ 6-fold-slower Koff a |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | spike glycoprotein |
| Uniprot protein ID | P59594 |
| Protein length | 1255 amino acids |
| Protein description | The spike protein of SARS coronaviruses is a protein composed of three polypeptide chains and it contains two domains, S1 and S2. The S1 domain binds the host cell receptors, while the S2 domain is responsible for the fusion of the virus with the host cell membrane. Between S1 and S2, there is a hinge region which is targeted by the host cell proteases. |
Literature information:
| Pubmed ID | 25231316 |
| Clinical information | No |
| Disease | - |
| Published year | 2014 |
| Journal | Journal of Virology |
| Title | Effects of human anti-spike protein receptor binding domain antibodies on severe acute respiratory syndrome coronavirus neutralization escape and fitness |
| Author | Jianhua Sui, Meagan Deming, Barry Rockx, Robert C Liddington, Quan Karen Zhu |
| Evidence | FIG 5 |