Mutation detail:
Mutation site | I529T |
Virus | MERS-CoV |
Mutation level ![]() |
Amino acid level |
Gene/protein/region type | S Protein |
Gene ID | 1489668 |
Country | South Korea |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | - |
Sample ![]() |
Human |
Variants | - |
Viral reference sequence | KT029139.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
promote |
Transmission mechanism | The microevolution of spike genes in MERS-CoV toward reduced human affinity but enhanced escape from neutralizing antibodies in a single patient might increase the probability of a spreading event by extending the virus replication period in the host. |
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 | 30900977 |
Clinical information | No |
Disease | - |
Published year | 2019 |
Journal | Emerging Infectious Diseases |
Title | Sequential Emergence and Wide Spread of Neutralization Escape Middle East Respiratory Syndrome Coronavirus Mutants, South Korea, 2015 |
Author | Yeon-Sook Kim, Abdimadiyeva Aigerim, Uni Park, Yuri Kim, Ji-Young Rhee |
Evidence | We focused on 2 mutations (D510G and I529T) in the RBD region. |