Mutation detail:
| Mutation site | S185T |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | India |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | clade 7 |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | FJ966082.1 |
| 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 | 27997573 |
| Clinical information | No |
| Disease | - |
| Published year | 2016 |
| Journal | PLoS One |
| Title | Genetic Characterization of Circulating 2015 A(H1N1)pdm16 Influenza Viruses from Eastern India |
| Author | Anupam Mukherjee,Mukti Kant Nayak,Shanta Dutta,Samiran Panda,Biswa Ranjan Satpathi |
| Evidence | the amino acid variations of S185T and T197A were observed in the 190 helix184-195 regions of predicted antigenic sites of all HA sequences reported during 2014-2015 along with the viruses analyzed in this study. |