Mutation detail:
| Mutation site | S162N |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | Spain |
| 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 | 29128380 |
| Clinical information | Yes |
| Disease | - |
| Published year | 2017 |
| Journal | Vaccine |
| Title | Low influenza vaccine effectiveness and the effect of previous vaccination in preventing admission with A(H1N1)pdm09 or B/VictoriaLineage in patients 60 years old or older during the 2015/2016 influenza season |
| Author | Joan Puig-Barbera,Beatriz Guglieri-Lopez,Miguel Tortajada-Girbes,F Xavier Lopez-Labrador,Mario Carballido-Fernandez |
| Evidence | All the isolates during the 2015/2016 influenza season belonged to the new clade 6B.1 and showed almost the same pattern of mutations as clade 6B viruses plus the specific ones for clade 6B.1,including the S162N mutation in the antigenic site Sa, which results in the formation of a new potential glycosylation motif at residues 162-164 of the hemagglutinin |