Mutation detail:
| Mutation site | G158E |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | FN434458.1 |
| Drug/antibody/vaccine | vaccine resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| 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 | 28631598 |
| Clinical information | No |
| Disease | - |
| Published year | 2017 |
| Journal | J Gen Virol |
| Title | In vitro and in vivo evidence of a potential A(H1N1)pdm22 antigenic drift mediated by escape mutations in the haemagglutinin Sa antigenic site |
| Author | Miguel Retamal,Yacine Abed,Chantal Rhéaume,Mariana Baz,Guy Boivin |
| Evidence | Of interest, six of the 11 aa substitutions found in our escape mutants were located in the predicted antigenic sites Cb(T80R; H3-numbering is used throughout the paper), Ca2(G143E), Sa(G158E, N159D and K166E) and Sb(A198E). |