Mutation detail:
| Mutation site | S179N |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | Thailand |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | clade 6B |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_026433.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Hemagglutinin |
| Uniprot protein ID | C3W627 |
| Protein length | 566 amino acids |
| Protein description | The HA protein is translated as an uncleaved HA0 precursor protein, folded as a trimer, and glycosylated and acylated. The HA protein binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. |
Literature information:
| Pubmed ID | 34070388 |
| Clinical information | Yes |
| Disease | - |
| Published year | 2021 |
| Journal | Viruses |
| Title | Molecular Characterization of Seasonal Influenza A and B from Hospitalized Patients in Thailand in 2018-2019 |
| Author | Kobporn Boonnak,Chayasin Mansanguan,Dennis Schuerch,Usa Boonyuen,Hatairat Lerdsamran |
| Evidence | Substitution at positions P100S, S101N, D114S, S179N, K180Q, S181T, T214A, S220T, and I233R were detected in the head domain of H1N1 strain isolates in this study. These mutations are common among the A/H1N1 global strains reported after pandemic 2009. Among these Thai strains, we found additional mutations at antigenic sites; S91R (Cb), S181T(Sa), and T202I (Sb) (Figure 2B). Moreover, a unique mutation (S200P) was observed at the receptor binding site |