Mutation detail:
| Mutation site | S90P |
| 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 | MK622934.1 |
| Drug/antibody/vaccine | - |
| 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 | 32699088 |
| Clinical information | No |
| Disease | - |
| Published year | 2020 |
| Journal | JOURNAL OF VIROLOGY |
| Title | N-Linked Glycan Sites on the Influenza A Virus Neuraminidase Head Domain Are Required for Efficient Viral Incorporation and Replication |
| Author | Henrik Östbye,Jin Gao,Mira Rakic Martinez,Hao Wang,Jan-Willem de Gier |
| Evidence | we were able to identify sequences that carry a mutation in one of the sites (S90P, T148A, and N235K). These natural mutations were introduced into an NA (N1-MI15) from a previously recommended 2009 pandemic-like H1N1 vaccine strain (A/Michigan/45/2015) in various combinations to determine if the conserved sites are required for H1N1 IAV replication. We chose N1-MI15 for the analysis, as it does not contain any variable head glycan sites. An additional mutation (S90A) was also included to alleviate potential folding concerns associated with the S90P mutation that introduces a Pro residue |