Mutation detail:
| Mutation site | Y442C |
| 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 | AY291315.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | Further mutational experiments identified two substitutions, Y442C and L472F, within the receptor binding domain that could be critical for the reduced S incorporation, as well as reduced binding affinity between the S protein and ACE2 receptor. |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| 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 | 18362400 |
| Clinical information | No |
| Disease | - |
| Published year | 2008 |
| Journal | Japanese Journal Of Infectious Diseases |
| Title | Reduced incorporation of SARS-CoV spike protein into viral particles due to amino acid substitutions within the receptor binding domain |
| Author | Shu-Ming Li, Gui-Mei Li, Shota Nakamura, Kazuyoshi Ikuta, Takaaki Nakaya |
| Evidence | Further mutational experiments identified two substitutions, Y442C and L472F, within the receptor binding domain that could be critical for the reduced S incorporation, as well as reduced binding affinity between the S protein and ACE2 receptor |