Mutation detail:
| Mutation site | N29S |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | NEP |
| Gene ID | 23308112 |
| Country | India |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | clade 6B |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | FJ966086.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Nuclear Export Protein |
| Uniprot protein ID | C3W610 |
| Protein length | 121 amino acids |
| Protein description | NEP can be divided into a protease-sensitive N-terminal domain (amino acids 1-53) and a protease-resistant C-terminal domain (amino acids 54-121), the crystal structure of which has been solved. NEP mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNPs to which the M1 protein is bound. Because the M1 protein is not available in large quantities until the later stages of infection, such an indirect recognition mechanism probably ensures that genomic RNPs are not exported from the nucleus before sufficient quantities of viral mRNA and progeny genomic RNA have been synthesized. Furthermore, the RNPs enters the cytoplasm only when they have associated with the M1 protein that is necessary to guide them to the plasma membrane. May down-regulate viral RNA synthesis when overproduced. |
Literature information:
| Pubmed ID | 27997573 |
| Clinical information | No |
| Disease | - |
| Published year | 2016 |
| Journal | PLoS One |
| Title | Genetic Characterization of Circulating 2015 A(H1N1)pdm47 Influenza Viruses from Eastern India |
| Author | Anupam Mukherjee,Mukti Kant Nayak,Shanta Dutta,Samiran Panda,Biswa Ranjan Satpathi |
| Evidence | a number of new mutations were observed in the NP (S498N), NS (NS1: K131E and N205S; NEP: N29S), PA (V100I, N321K, I330V and R362K), PB1 (G154D), and PB2 (R54K, M66I, D195N, R293K and V734I) sequences |