Mutation detail:
| Mutation site | K27A |
| Virus | MERS-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 | JX869059.2 |
| Drug/antibody/vaccine | mAb-G2 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 | K9N5Q8 |
| Protein length | 1353 amino acids |
| Protein description | The spike protein of 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. The S1 is composed of an N-terminal domain (S1-NTD) which binds sugar and protein receptors, and a C- terminal domain (S1-CTD) which is responsible for binding host cell protein receptors. The S2 binds to the S1-NTD, contains heptad hydrophobic) repeat regions and a fusion peptide which is located downstream of S1-NTD. |
Literature information:
| Pubmed ID | 31553909 |
| Clinical information | No |
| Disease | - |
| Published year | 2019 |
| Journal | Cell Reports |
| Title | Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD |
| Author | Nianshuang Wang,Osnat Rosen,Lingshu Wang,Hannah L Turner,Laura J Stevens |
| Evidence | In addition to these two escape mutations, we further probed the interface by introducing single mutations K27A or S191A into the S1-NTD. As expected from the structure, either of these two substitutions largely abolished the binding to G2 Fab (Figure S2A |