Mutation detail:
| Mutation site | H275Y |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | NA |
| Gene ID | 23308118 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | FJ966084.1 |
| Drug/antibody/vaccine | oseltamivir resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| 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 | 21635924 |
| Clinical information | No |
| Disease | - |
| Published year | 2011 |
| Journal | Antiviral Research |
| Title | Assessment of the efficacy of the neuraminidase inhibitor oseltamivir against 2009 pandemic H1N1 influenza virus in ferrets |
| Author | Elena A Govorkova,Bindumadhav M Marathe,Ashley Prevost,Jerold E Rehg,Robert G Webster |
| Evidence | A single H275Y NA mutation is the most common cause of resistance in the N1 NA subtype and has been observed in oseltamivir-resistant H1N1pdm viruses (Deyde et al., 2010).A novel I223R NA mutation identified in H1N1pdm viruses caused relatively modest resistance to both oseltamivir and zanamivir;in combination with H275Y, this mutation significantly increased resistance to oseltamivir and peramivir but only marginally increased resistance to zanamivir |