Mutation detail:
| Mutation site | I123V |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | NS1 |
| Gene ID | 23308111 |
| Country | Mexico |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_026432.1 |
| Drug/antibody/vaccine | Adamantane resistant |
| 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 | 19465683 |
| Clinical information | No |
| Disease | - |
| Published year | 2009 |
| Journal | Science |
| Title | Antigenic and Genetic Characteristics of the Early Isolates of Swine-Origin 2009 A(H1N1) Influenza Viruses Circulating in Humans |
| Author | Rebecca J. Garten,C. Todd Davis,Colin A. Russell,Bo Shu,Stephen Lindstrom |
| Evidence | Analysis across the genomes of the 2009 A(H1N1) viruses from Mexico and the USA to date, found five minor genome variants: (i) the consensus sequence, (ii) T373I mutation in the NP paired with M582L mutation in the PA, (iii) amino acid substitutions of V106I and N247D in the NA (N2 numbering) paired with V100I in the NP and (iv) amino acid substitutions of S206T in the HA1 (H3 numbering) clustering with both V106I and N247D in the NA (N2 numbering), V100I in the NP and I123V in the NS1, and (v) amino acid substitutions of S91P, V323I (H3 numbering) together with S224P in the PA (Table S2). |