Mutation detail:
| Mutation site | N294S |
| 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 | LC333187.1 |
| Drug/antibody/vaccine | zanamivir resistant, oseltamivir resistant, peramivir 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 | 28951584 |
| Clinical information | No |
| Disease | - |
| Published year | 2017 |
| Journal | Scientific Reports |
| Title | Identification of neuraminidase inhibitors against dual H274Y/I222R mutant strains |
| Author | Kai-Cheng Hsu,Hui-Chen Hung,Wei-Chun HuangFu,Tzu-Ying Sung,Tony Eight Lin |
| Evidence | Previous virtual screening approaches have been applied to NCI molecular library30,31. Cheng et al. identified potential novel antiviral compounds from NCI library30, which need to be further validated by assays. Hoffmann et al. discovered a series of diazenylaryl sulfonic acids as NA inhibitors, which inhibited N1 NA with drug-resistant mutations31, including H274Y, N294S, Y155H, Q136L, I427Q and I427M. |