Mutation detail:
| Mutation site | R441A |
| 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 | - |
| Transmissibility |
hinder |
| Transmission mechanism | We also demonstrated that the RBD-Fc bearing R441A mutation could not bind to soluble and cell-associated angiotensin-converting enzyme 2 (ACE2), the functional receptor for SARS-CoV and failed to block S protein-mediated pseudovirus entry, indicating tha |
| 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 | 16615996 |
| Clinical information | No |
| Disease | - |
| Published year | 2006 |
| Journal | Biochemical and Biophysical Research Communications |
| Title | A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity |
| Author | Yuxian He, Jingjing Li, Shibo Jiang |
| Evidence | We also demonstrated that the RBD-Fc bearing R441A mutation could not bind to soluble and cell-associated angiotensin-converting enzyme 2 (ACE2), the functional receptor for SARS-CoV and failed to block S protein-mediated pseudovirus entry, indicating tha |