Mutation detail:
| Mutation site | D222N |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | Ukraine |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC_026433.1 |
| Drug/antibody/vaccine | oseltamivir resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
increase |
| Pathogenicity mechanism | Correspondingly, viruses harboring these NS1 mutations exhibited increased virulence in mouse models of influenza.Mutation N321K in PA occurred in all isolates and confers increased virulence [48]. The NP mutation M105T is in a motif under selective press |
| 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 | 34834932 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Viruses |
| Title | Genotypic Variants of Pandemic H1N1 Influenza A Viruses Isolated from Severe Acute Respiratory Infections in Ukraine during the 2015/16 Influenza Season |
| Author | Oksana Zolotarova,Anna Fesenko,Olga Holubka,Larysa Radchenko,Eric Bortz |
| Evidence | Two other A(H1N1)pdm09 strains reported in Ukraine in the 2015/16 season, A/Dnipro/580/2016 and A/Ukraine/7182/2016, contained mutations D222G and D222N in HA, respectively, that are associated with severe disease outcome in patients |