Mutation detail:
| Mutation site | S206T |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | Lebanon |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_026434.1 |
| Drug/antibody/vaccine | amantadine-resistant |
| Transmissibility |
promote |
| Transmission mechanism | This strain was successful in continuous circulation, suggesting that it has a better transmission and infection efficiency than older viruses do, but the mechanisms responsible for this are still unknown |
| 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 | 21565547 |
| Clinical information | No |
| Disease | - |
| Published year | 2011 |
| Journal | J Clin Virol |
| Title | Genetic diversity and antiviral drug resistance of pandemic H1N1 2014 in Lebanon |
| Author | Hassan Zaraket,Hiroki Kondo,Carelle Tabet,Rima Hanna-Wakim,Yasushi Suzuki |
| Evidence | The S206T and D225E mutations occur in the HA receptor-binding domain and in antigenic sites Ca1 and Ca2, respectively |