Mutation detail:
| Mutation site | V555A |
| 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 |
Human |
| Variants | - |
| Viral reference sequence | JX869059.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | Furthermore, in patch 2, a single-residue substitution of either L506A or W553A, expected to alter the hydrophobic core (Figure 3C), significantly reduced both binding and viral entry efficiency (Figure 4). In particular, combined residue substitutions in |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| 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 | 23835475 |
| Clinical information | No |
| Disease | - |
| Published year | 2013 |
| Journal | Cell Research |
| Title | Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4 |
| Author | Nianshuang Wang, Xuanling Shi, Liwei Jiang, Senyan Zhang, Dongli Wang |
| Evidence | Figure 4 |