Mutation detail:
| Mutation site | H275Y |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | NA |
| Gene ID | 23308118 |
| Country | UK |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | clade 2B |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | EF566040.1 |
| Drug/antibody/vaccine | oseltamivir resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
decrease |
| Pathogenicity mechanism | It was consistently shown that the viability and pathogenicity of A/H1N1 viruses with the H275Y mutation were severely compromised both in vitro and in vivo compared with the viability and pathogenicity of the corresponding wild type (15,17) |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Neuraminidase |
| Uniprot protein ID | C3W6G3 |
| Protein length | 469 amino acids |
| Protein description | The NA assembles as a tetramer of four identical polypeptides and, when embedded in the envelope of the virus, accounts for approximately 10-20% of the total glycoproteins on the virion surface, with about 40-50 NA spikes and 300-400 HA spikes on an average sized virion of 120 nm. The four monomers, each of approximately 470 amino acids, fold into four distinct structural domains: the cytoplasmic tail, the transmembrane region, the stalk, and the catalytic head. The NA catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. |
Literature information:
| Pubmed ID | 20129961 |
| Clinical information | No |
| Disease | - |
| Published year | 2010 |
| Journal | J Clin Microbiol |
| Title | Genetic makeup of amantadine-resistant and oseltamivir-resistant human influenza A/H1N1 viruses |
| Author | Hassan Zaraket,Reiko Saito,Yasushi Suzuki,Tatiana Baranovich,Clyde Dapat |
| Evidence | Phylogenetic analysis revealed that the oseltamivir-resistant strain evolved from a reassortant oseltamivir-susceptible strain (clade 2B) which circulated in the 2007-2008 season by acquiring the H275Y resistance-conferring mutation in the NA gene. |