Mutation detail:
Mutation site | F103S |
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 ![]() |
Human |
Variants | - |
Viral reference sequence | GQ168862.1 |
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 | 21094080 |
Clinical information | No |
Disease | - |
Published year | 2011 |
Journal | J Clin Virol |
Title | Investigation of causes of oseltamivir chemoprophylaxis failures during influenza A (H1N1-2017) outbreaks |
Author | Vernon J Lee,Jonathan Yap,Sebastian Maurer-Stroh,Raphael T C Lee,Frank Eisenhaber |
Evidence | From the whole genome sequencing, several mutations at the HA (T220S, E275V, T333A, D240G);PB2 (K660R, L607V, V292I);NS1 (F103S), and NP (W104G) gene segments were detected, but none of them were likely to result in anti-viral resistance. |