Mutation detail:
| Mutation site | D1128A |
| 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 | AY278491.2 |
| Drug/antibody/vaccine | Mab 1A9 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 | 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 | 25019613 |
| Clinical information | No |
| Disease | - |
| Published year | 2014 |
| Journal | PLoS One |
| Title | Substitution at aspartic acid 1128 in the SARS coronavirus spike glycoprotein mediates escape from a S2 domain-targeting neutralizing monoclonal antibody |
| Author | Oi-Wing Ng, Choong-Tat Keng, Cynthia Sau-Wai Leung, J S Malik Peiris, Leo Lit Man Poon |
| Evidence | S protein containing the substitution of D1128 with alanine (D1128A) exhibited a significant decrease in binding capability to mAb 1A9 compared to wild-type S protein |