Mutation detail:
| Mutation site | P164S |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | NS1 |
| Gene ID | 23308111 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | CY010788.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Nonstructural Protein 1 |
| Uniprot protein ID | C3W611 |
| Protein length | 219 amino acids |
| Protein description | The non-structural protein 1 (NS1) is a crucial influenza A virus immune regulator that antagonizes antiviral response. The NS1 protein counteracts the production of IFNs and the activities of IFN-induced proteins that restrict influenza virus replication. Furthermore, NS1 is a multifunctional regulatory viral protein that plays a critical role as a posttranscriptional regulatory factor in the life cycle of influenza virus; specifically, binding virion RNA. NS1 protein consists of 2 distinct functional domains connected by a flexible linker region (LR): an N-terminal RNA- binding domain (RBD, aa 1-73) and a C-terminal effector domain (ED, aa 74-207). The nucleotide sequence (NLS) (aa 35-41) overlaps the sequences needed for dsRNA binding. |
Literature information:
| Pubmed ID | 25793397 |
| Clinical information | No |
| Disease | - |
| Published year | 2015 |
| Journal | PLoS One |
| Title | Characterization of a novel mutation in NS1 protein of influenza A virus induced by a chemical substance for the attenuation of pathogenicity |
| Author | Kohei Sasaki,Kyoko Hayashi,Jung-Bum Lee,Fumiya Kurosaki,Toshimitsu Hayashi |
| Evidence | From these results it can be shown that the mutation, NS1P164S, might be one of the key residues to control NS1 function concerning the induction of apoptosis. |